|
Name |
Accession |
Description |
Interval |
E-value |
| PaaN-DH |
TIGR02278 |
phenylacetic acid degradation protein paaN; This enzyme is proposed to act in the ring-opening ... |
4-674 |
0e+00 |
|
phenylacetic acid degradation protein paaN; This enzyme is proposed to act in the ring-opening step of phenylacetic acid degradation which follows ligation of the acid with coenzyme A (by PaaF) and hydroxylation by a multicomponent non-heme iron hydroxylase complex (PaaGHIJK). Gene symbols have been standardized in. This enzyme is related to aldehyde dehydrogenases and has domains which are members of the pfam00171 and pfam01575 families. This family includes paaN genes from Pseudomonas, Sinorhizobium, Rhodopseudomonas, Escherichia, Deinococcus and Corynebacterium. Another homology family (TIGR02288) includes several other species.
Pssm-ID: 131331 [Multi-domain] Cd Length: 663 Bit Score: 1160.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 4 LASFLSGTWQSGRGRSRLIHHAISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFY 83
Cdd:TIGR02278 1 LQSYLSGEWRTGQGEGVPVRDASTGEVLARVTSEGLDVAAAVAWAREVGGPALRALTFHERARMLKALAQYLSERKEALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 84 ALSAQTGATRADSWVDIEGGIGTLFTYASLGSRELPDDTLWPEDELIPLSKEGGFAARHVLTSKSGVAVHINAFNFPCWG 163
Cdd:TIGR02278 81 ALAATTGATRRDNWVDIDGGIGTLFTYSSLGRRELPDANLIPEDEFEPLSKDGSFQGRHILTPKGGVAVQINAFNFPVWG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 164 MLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLVPEGAISLICGSAGDLLDHLDSQDVVTFTGSAATGQMLRVQ 243
Cdd:TIGR02278 161 LLEKFAPAFLAGVPTLAKPATPTAYVAEALVRTMVESGLLPEGSLQLICGSAGDLLDHLDHRDVVAFTGSAATADRLRAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 244 PNIVAKSIPFTMEADSLNCCVLGEDITPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVV 323
Cdd:TIGR02278 241 PNVLERGIRFNAEADSLNAAILGEDATPDEPEFDLFAQEIVRELTIKAGQKCTAIRRVIVPKALLEAVLKALQARLAKVV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 324 VGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLSaaGAFFPPTLLYCPQPDeTPAVHATEAFGPVATL 403
Cdd:TIGR02278 321 LGDPREEGVDMGPLVSLEQRADVEAAVAALLAAGAEVRLGGPGRLD--GAFFPPTLLLAEDPW-AGAVHATEAFGPVATF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 404 MPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIADAARTHGRIQILNEESAKESTGHGSPLPQLVHGGPGRAGGGEE 483
Cdd:TIGR02278 398 FPYGDRAEAARLAARGGGSLVATLATSDPEEARQFILGLAPYHGRLHILNRDDAAESTGHGSPLPRLLHGGPGRAGGGEE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 484 LGGLRAVKHYMQRTAVQGSPTMLAAISKQWVRGAKVEEDRIHPFRKYFEELQPGDSLLTPRRTMTEADIVNFACLSGDHF 563
Cdd:TIGR02278 478 LGGLRSVKHYMQRTAIQGSPWLLAALTGQWARGAEVPGAEVHPFRKPYEDLEIGDSLTTHRRTVTEADIALFAALSGDHF 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 564 YAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGVGPVIANYGLENLRFIEPVKPGDTIQVRLTCKRKTLKKQRSAee 643
Cdd:TIGR02278 558 YAHMDEIAARESFFGKRVAHGYFVLSAAAGLFVDPAPGPVLANYGLENLRFLEPVGPGDTIQVRLTVKRKTPRDEKTY-- 635
|
650 660 670
....*....|....*....|....*....|.
gi 1744921533 644 kptGVVEWAVEVFNQHQTPVALYSILTLVAR 674
Cdd:TIGR02278 636 ---GVVEWAAEVVNQNGEPVATYDVLTLVAR 663
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
4-511 |
0e+00 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 853.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 4 LASFLSGTWQSGRGRSRLIHHAISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFY 83
Cdd:cd07128 1 LQSYVAGQWHAGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 84 ALSAQTGATRADSWVDIEGGIGTLFTYASLGSRELPDDTLWPEDELIPLSKEGGFAARHVLTSKSGVAVHINAFNFPCWG 163
Cdd:cd07128 81 ALSAATGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVEPLSKDGTFVGQHILTPRRGVAVHINAFNFPVWG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 164 MLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLVPEGAISLICGSAGDLLDHLDSQDVVTFTGSAATGQMLRVQ 243
Cdd:cd07128 161 MLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLLPEGALQLICGSVGDLLDHLGEQDVVAFTGSAATAAKLRAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 244 PNIVAKSIPFTMEADSLNCCVLGEDITPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVV 323
Cdd:cd07128 241 PNIVARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 324 VGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAgCEIRLGGQADL------SAAGAFFPPTLLYCPQPDETPAVHATEAF 397
Cdd:cd07128 321 VGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGPDRFevvgadAEKGAFFPPTLLLCDDPDAATAVHDVEAF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 398 GPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIADAARTHGRIQILNEESAKESTGHGSPLPQLVHGGPGR 477
Cdd:cd07128 400 GPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPYHGRLLVLNRDSAKESTGHGSPLPQLVHGGPGR 479
|
490 500 510
....*....|....*....|....*....|....
gi 1744921533 478 AGGGEELGGLRAVKHYMQRTAVQGSPTMLAAISK 511
Cdd:cd07128 480 AGGGEELGGLRGVKHYMQRTAVQGSPTMLTAITG 513
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
1-510 |
0e+00 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 559.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 1 MQQLASFLSGTWQSGRGRSRLIHHAISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKE 80
Cdd:PRK11903 2 TELLANYVAGRWQAGSGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 81 RFYALS-AQTGATRADSWVDIEGGIGTLFTYASLGsRELPDDTLWPEDELIPLSKEGGFAARHVLTSKSGVAVHINAFNF 159
Cdd:PRK11903 82 AYYDIAtANSGTTRNDSAVDIDGGIFTLGYYAKLG-AALGDARLLRDGEAVQLGKDPAFQGQHVLVPTRGVALFINAFNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 160 PCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLVPEGAISLICGSAGDLLDHLDSQDVVTFTGSAATGQM 239
Cdd:PRK11903 161 PAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGILPAGALSVVCGSSAGLLDHLQPFDVVSFTGSAETAAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 240 LRVQPNIVAKSIPFTMEADSLNCCVLGEDITPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARL 319
Cdd:PRK11903 241 LRSHPAVVQRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 320 QKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTlLAAGCEIRLGG------QADlSAAGAFFPPTLLYCPQPDETPAVHA 393
Cdd:PRK11903 321 AKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGggfalvDAD-PAVAACVGPTLLGASDPDAATAVHD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 394 TEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIADAARTHGRIQILNEESAKESTGHGSPLPQLVHG 473
Cdd:PRK11903 399 VEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADSHGRVHVISPDVAALHTGHGNVMPQSLHG 478
|
490 500 510
....*....|....*....|....*....|....*..
gi 1744921533 474 GPGRAGGGEELGGLRAVKHYMQRTAVQGSPTMLAAIS 510
Cdd:PRK11903 479 GPGRAGGGEELGGLRALAFYHRRSAVQASPAVLDALT 515
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-451 |
2.69e-91 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 292.03 E-value: 2.69e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 2 QQLASFLSGTWQSGRGRSRL-IHHAISGEALWEV---TSEGLDMA--AARlfaieKGAPALRAMTFIERAAMLKAVAKHL 75
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFdVINPATGEVLARVpaaTAEDVDAAvaAAR-----AAFPAWAATPPAERAAILLRAADLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 76 LSEKERFYAL-SAQTGATRADSWVDIEGGIGTLFTYASLGSRelpddtlwPEDELIPLSKEGGFAaRHVLTSKsGVAVHI 154
Cdd:COG1012 79 EERREELAALlTLETGKPLAEARGEVDRAADFLRYYAGEARR--------LYGETIPSDAPGTRA-YVRREPL-GVVGAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 155 NAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGS---AGDLLDHLDSQDVVTFT 231
Cdd:COG1012 149 TPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGL-PAGVLNVVTGDgseVGAALVAHPDVDKISFT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 232 GSAATGQMLRVQPNivAKSIPFTMEADSLNCCVLGEDItpdqpEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAV 311
Cdd:COG1012 228 GSTAVGRRIAAAAA--ENLKRVTLELGGKNPAIVLDDA-----DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 312 SDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLSAAGAFFPPTLLYCPQPDETpaV 391
Cdd:COG1012 301 VERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLADVTPDMR--I 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 392 HATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFiADAARtHGRIQI 451
Cdd:COG1012 379 AREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRV-ARRLE-AGMVWI 436
|
|
| MaoC_C |
cd03452 |
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ... |
530-676 |
3.17e-87 |
|
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family.
Pssm-ID: 239536 [Multi-domain] Cd Length: 142 Bit Score: 269.27 E-value: 3.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 530 YFEELQPGDSLLTPRRTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGVGPVIANYGL 609
Cdd:cd03452 1 NLEQLRPGDSLLTHRRTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFVDPAPGPVLANYGL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1744921533 610 ENLRFIEPVKPGDTIQVRLTCKRKTLKkqrsaEEKPTGVVEWAVEVFNQHQTPVALYSILTLVARQH 676
Cdd:cd03452 81 ENLRFLEPVYPGDTIQVRLTCKRKIPR-----DGQDYGVVRWDAEVTNQNGELVASYDILTLVAKKG 142
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
42-440 |
3.92e-65 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 221.31 E-value: 3.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 42 AAARlfaieKGAPALRAMTFIERAAMLKAVAKhLLSEKERFYA--LSAQTGATRADSWVDIEGGIGTLFTYASLGSRelp 119
Cdd:cd07078 5 AAAR-----AAFKAWAALPPAERAAILRKLAD-LLEERREELAalETLETGKPIEEALGEVARAADTFRYYAGLARR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 120 ddtlWPEDELIPLSkeGGFAARHVLTSKsGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVD 199
Cdd:cd07078 76 ----LHGEVIPSPD--PGELAIVRREPL-GVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 200 SGLvPEGAISLICGSAGDLLDHLDSQ---DVVTFTGSAATGQMLRvqpNIVAKS-IPFTMEADSLNCCVLGEDitpdqPE 275
Cdd:cd07078 149 AGL-PPGVLNVVTGDGDEVGAALASHprvDKISFTGSTAVGKAIM---RAAAENlKRVTLELGGKSPLIVFDD-----AD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 276 FALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLA 355
Cdd:cd07078 220 LDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 356 AGCEIRLGGQADLSAAGAFFPPTLLYCPQPDETpaVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIA 435
Cdd:cd07078 300 EGAKLLCGGKRLEGGKGYFVPPTVLTDVDPDMP--IAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERA 377
|
....*
gi 1744921533 436 RQFIA 440
Cdd:cd07078 378 LRVAE 382
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
42-472 |
4.98e-58 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 202.47 E-value: 4.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 42 AAARLFAiEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYALSAQTGATRADSWVDIEGGIGTLFTYASLG-SRELPD 120
Cdd:cd07084 2 ERALLAA-DISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIySYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 121 DTLWPedelipLSKEGGFAARHVLtSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDS 200
Cdd:cd07084 81 EPGNH------LGQGLKQQSHGYR-WPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 201 GLVPEGAISLICGS---AGDLLDHLDSqDVVTFTGSAATGQMLRVQPnivaKSIPFTMEADSLNCCVLGeditPDQPEFA 277
Cdd:cd07084 154 GLLPPEDVTLINGDgktMQALLLHPNP-KMVLFTGSSRVAEKLALDA----KQARIYLELAGFNWKVLG----PDAQAVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 278 LFIREVVREMTTKAGQKCTAIRRIIVPQAL-VNAVSDALVARLQKVVVGDpaqegvkmgALVNAEQRADVQEKVNTLLAA 356
Cdd:cd07084 225 YVAWQCVQDMTACSGQKCTAQSMLFVPENWsKTPLVEKLKALLARRKLED---------LLLGPVQTFTTLAMIAHMENL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 357 GCEIRLGGQADLSAAGAFF-------PPTLLYCPQPDETPAVHATEAFGPVATLMPAQNQQ--HALQLACAGGGSLAGTL 427
Cdd:cd07084 296 LGSVLLFSGKELKNHSIPSiygacvaSALFVPIDEILKTYELVTEEIFGPFAIVVEYKKDQlaLVLELLERMHGSLTAAI 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1744921533 428 VTADPQIARQFIADAARtHGRIQILNeesakesTGHGSPLPQLVH 472
Cdd:cd07084 376 YSNDPIFLQELIGNLWV-AGRTYAIL-------RGRTGVAPNQNH 412
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
12-441 |
5.78e-57 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 200.06 E-value: 5.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 12 WQSGRGRSRLIHHAISGEALWEV---TSEGLDMAAArlfAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERF-YALSA 87
Cdd:pfam00171 1 WVDSESETIEVINPATGEVIATVpaaTAEDVDAAIA---AARAAFPAWRKTPAAERAAILRKAADLLEERKDELaELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 88 QTGATRADSWVDIEGGIGTLFTYASLGSRelpddtlwPEDELIPLSK-EGGFAARHVLtsksGVAVHINAFNFPCWGMLE 166
Cdd:pfam00171 78 ENGKPLAEARGEVDRAIDVLRYYAGLARR--------LDGETLPSDPgRLAYTRREPL----GVVGAITPWNFPLLLPAW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 167 KLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHL-DSQDV--VTFTGSAATGQ----- 238
Cdd:pfam00171 146 KIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGL-PAGVLNVVTGSGAEVGEALvEHPDVrkVSFTGSTAVGRhiaea 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 239 ----MLRVQ-------PNIVAKSipftmeADslnccvlgeditpdqpeFALFIREVVREMTTKAGQKCTAIRRIIVPQAL 307
Cdd:pfam00171 225 aaqnLKRVTlelggknPLIVLED------AD-----------------LDAAVEAAVFGAFGNAGQVCTATSRLLVHESI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 308 VNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLsAAGAFFPPTLLYCPQPDE 387
Cdd:pfam00171 282 YDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEAGL-DNGYFVEPTVLANVTPDM 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1744921533 388 TpaVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIAD 441
Cdd:pfam00171 361 R--IAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARR 412
|
|
| MaoC |
COG2030 |
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism]; |
530-674 |
9.61e-47 |
|
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
Pssm-ID: 441633 [Multi-domain] Cd Length: 140 Bit Score: 161.98 E-value: 9.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 530 YFEELQPGDSLLTPRRTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGVGPVIANYGL 609
Cdd:COG2030 1 YFEDLEVGDVLPHGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLGL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1744921533 610 ENLRFIEPVKPGDTIQVRLTCKRKTlkkqrsaEEKPTGVVEWAVEVFNQHQTPVALYSILTLVAR 674
Cdd:COG2030 81 QEVRFLRPVRVGDTLRARVEVLEKR-------ESKSRGIVTLRTTVTNQDGEVVLTGEATVLVPR 138
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
7-435 |
3.32e-43 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 162.05 E-value: 3.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 7 FLSGTWQSGRGRSRL-IHHAISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKhLLSEKERFYA- 84
Cdd:cd07088 1 YINGEFVPSSSGETIdVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLAD-LIRENADELAk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 85 -LSAQTGATRADSWVDIEGGIgTLFTYASLGSRELpddtlwpEDELIPLSKEGgfaaRHVLTSKS--GVAVHINAFNFPC 161
Cdd:cd07088 80 lIVEEQGKTLSLARVEVEFTA-DYIDYMAEWARRI-------EGEIIPSDRPN----ENIFIFKVpiGVVAGILPWNFPF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 162 WGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHLDSQ---DVVTFTGSAATGQ 238
Cdd:cd07088 148 FLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGL-PAGVLNIVTGRGSVVGDALVAHpkvGMISLTGSTEAGQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 239 --MLRVQPNIVAKSI------PFTMEADSlnccvlgeDItpdqpEFAlfIREVVREMTTKAGQKCTAIRRIIVPQALVNA 310
Cdd:cd07088 227 kiMEAAAENITKVSLelggkaPAIVMKDA--------DL-----DLA--VKAIVDSRIINCGQVCTCAERVYVHEDIYDE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 311 VSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLSAAGAFFPPTLLYCPQPDETpa 390
Cdd:cd07088 292 FMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDME-- 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1744921533 391 VHATEAFGPVATLMPAQNQQHALQLA--CAGGgsLAGTLVTADPQIA 435
Cdd:cd07088 370 IVQEEIFGPVLPVVKFSSLDEAIELAndSEYG--LTSYIYTENLNTA 414
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
27-439 |
1.56e-41 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 156.99 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTGATRADSWVDIEGGIG 105
Cdd:cd07149 8 DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTiALEAGKPIKDARKEVDRAIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 106 TlFTYASLGSRELPDdtlwpedELIPLSKEGGFAARHVLTSKS--GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPA 183
Cdd:cd07149 88 T-LRLSAEEAKRLAG-------ETIPFDASPGGEGRIGFTIREpiGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 184 TATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHLDSQD---VVTFTGSAATGQMLRVQPNIvaKSIpfTMEADSl 260
Cdd:cd07149 160 SQTPLSALKLAELLLEAGL-PKGALNVVTGSGETVGDALVTDPrvrMISFTGSPAVGEAIARKAGL--KKV--TLELGS- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 261 NCCVlgedITPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNA 340
Cdd:cd07149 234 NAAV----IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 341 EQRADVQEKVNTLLAAGCEIRLGGQADlsaaGAFFPPTLLYcpQPDETPAVHATEAFGPVATLMPAQNQQHALQLACAGG 420
Cdd:cd07149 310 AEAERIEEWVEEAVEGGARLLTGGKRD----GAILEPTVLT--DVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSP 383
|
410
....*....|....*....
gi 1744921533 421 GSLAGTLVTADPQIARQFI 439
Cdd:cd07149 384 YGLQAGVFTNDLQKALKAA 402
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
35-444 |
1.33e-39 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 151.73 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 35 TSEGLDMA--AARlfaieKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYALSAQ-TGATRADSWVDIEGGIGTLFTYA 111
Cdd:cd07110 17 TAEDVDAAvrAAR-----RAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARdNGKPLDEAAWDVDDVAGCFEYYA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 112 SLGsrELPDDTLwpeDELIPLSKEGgFAArHVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQ 191
Cdd:cd07110 92 DLA--EQLDAKA---ERAVPLPSED-FKA-RVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 192 AMVKSIVDSGLvPEGAISLICG---SAGDLLDHLDSQDVVTFTGSAATGQmlRVQPNIVAKSIPFTMEADSLNCCVLGED 268
Cdd:cd07110 165 ELAEIAAEAGL-PPGVLNVVTGtgdEAGAPLAAHPGIDKISFTGSTATGS--QVMQAAAQDIKPVSLELGGKSPIIVFDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 269 ITPDQP-EFALFirevvrEMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQ 347
Cdd:cd07110 242 ADLEKAvEWAMF------GCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 348 EKVNTLLAAGCEIRLGGQ-ADLSAAGAFFPPTLLYCPQPDEtpAVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGT 426
Cdd:cd07110 316 SFIARGKEEGARLLCGGRrPAHLEKGYFIAPTVFADVPTDS--RIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAA 393
|
410
....*....|....*...
gi 1744921533 427 LVTADPQIARQFiADAAR 444
Cdd:cd07110 394 VISRDAERCDRV-AEALE 410
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
42-431 |
4.29e-39 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 150.19 E-value: 4.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 42 AAARLF--AIEKGAPALRAMTFIERAAMLKAVAKHLLSekerfyALSAQTGATRADSWVDIEGGIGTLFTYASLgSRELP 119
Cdd:cd07120 27 AARRAFdeTDWAHDPRLRARVLLELADAFEANAERLAR------LLALENGKILGEARFEISGAISELRYYAGL-ARTEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 120 DDTLWPEDELIPLskeggfaarhVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVD 199
Cdd:cd07120 100 GRMIEPEPGSFSL----------VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 200 SGLVPEGAISLICGSAGDLLDHLDSQ---DVVTFTGSAATGQmlRVQPNIVAKSIPFTMEADSLNCCVLGEDitpdqPEF 276
Cdd:cd07120 170 IPSLPAGVVNLFTESGSEGAAHLVASpdvDVISFTGSTATGR--AIMAAAAPTLKRLGLELGGKTPCIVFDD-----ADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 277 ALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAA 356
Cdd:cd07120 243 DAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAA 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1744921533 357 GCEI--RLGGQADLSAAGAFFPPTLLYCPQPDeTPAVHaTEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTAD 431
Cdd:cd07120 323 GAEVvlRGGPVTEGLAKGAFLRPTLLEVDDPD-ADIVQ-EEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
22-416 |
4.68e-39 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 150.28 E-value: 4.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 22 IHHAISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYA-LSAQTGATRADSWVDI 100
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKiIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 101 EGGIGTLFTYASLGSRElpddtlwpEDELIPLSKEGGFAARHVLTSKS--GVAVHINAFNFPCWGMLEKLAPTWLGGMPA 178
Cdd:cd07094 83 DRAIDTLRLAAEEAERI--------RGEEIPLDATQGSDNRLAWTIREpvGVVLAITPFNFPLNLVAHKLAPAIATGCPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 179 IIKPATATAQLTQAMVKSIVDSGlVPEGAISLICGSAGDLLDHL---DSQDVVTFTGSAATGQMLRVQPNIvaKSIpfTM 255
Cdd:cd07094 155 VLKPASKTPLSALELAKILVEAG-VPEGVLQVVTGEREVLGDAFaadERVAMLSFTGSAAVGEALRANAGG--KRI--AL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 256 EADSLNCCVLGEDITPDQPefalfIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMG 335
Cdd:cd07094 230 ELGGNAPVIVDRDADLDAA-----IEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 336 ALVNAEQRADVQEKVNTLLAAGCEIRLGGQADlsaaGAFFPPTLLYCPQPDeTPAVHaTEAFGPVATLMPAQNQQHALQL 415
Cdd:cd07094 305 PLISEEAAERVERWVEEAVEAGARLLCGGERD----GALFKPTVLEDVPRD-TKLST-EETFGPVVPIIRYDDFEEAIRI 378
|
.
gi 1744921533 416 A 416
Cdd:cd07094 379 A 379
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-442 |
6.55e-39 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 150.09 E-value: 6.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 6 SFLSGTWQSGRGRSRLIHHAISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYAL 85
Cdd:cd07097 3 NYIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 86 SA-QTGATRADSWVDIEGGIGTLFTYASLGSReLPDDTLWPEDELIplskeggfaarHVLTSKS--GVAVHINAFNFP-- 160
Cdd:cd07097 83 LTrEEGKTLPEARGEVTRAGQIFRYYAGEALR-LSGETLPSTRPGV-----------EVETTREplGVVGLITPWNFPia 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 161 --CWgmleKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGD----LLDHlDSQDVVTFTGSA 234
Cdd:cd07097 151 ipAW----KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGL-PAGVFNLVMGSGSEvgqaLVEH-PDVDAVSFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 235 ATGqmLRVQPNIVAKSIPFTMEADSLNCCVLGEDitpdqPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDA 314
Cdd:cd07097 225 AVG--RRIAAAAAARGARVQLEMGGKNPLVVLDD-----ADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 315 LVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQA-DLSAAGAFFPPTLLYCPQPDETPAvhA 393
Cdd:cd07097 298 LVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlKRPDEGYYLAPALFAGVTNDMRIA--R 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1744921533 394 TEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIADA 442
Cdd:cd07097 376 EEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRV 424
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
42-440 |
1.05e-37 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 144.29 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 42 AAARlfaieKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTGATRADSWVDIEGGIGTLFTYASLGSRelpd 120
Cdd:cd06534 1 AAAR-----AAFKAWAALPPAERAAILRKIADLLEERREELAALeTLETGKPIEEALGEVARAIDTFRYAAGLADK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 121 dtlWPEDELIPLSKegGFAARHVLTSKsGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDS 200
Cdd:cd06534 72 ---LGGPELPSPDP--GGEAYVRREPL-GVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 201 GLvPEGAISLICGS---AGDLLDHLDSQDVVTFTGSAATGQMLRvqpNIVAKS-IPFTMEADSLNCCVLGEDitpdqPEF 276
Cdd:cd06534 146 GL-PPGVVNVVPGGgdeVGAALLSHPRVDKISFTGSTAVGKAIM---KAAAENlKPVTLELGGKSPVIVDED-----ADL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 277 ALFIREVVREMTTKAGQKCTAIRRIIVPQalvnAVSDALVARLQKVVVgdpaqegvkmgalvnaeqradvqekvntllaa 356
Cdd:cd06534 217 DAAVEGAVFGAFFNAGQICTAASRLLVHE----SIYDEFVEKLVTVLV-------------------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 357 gceirlggqadlsaagaffpptllycPQPDETPAVHaTEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIAR 436
Cdd:cd06534 261 --------------------------DVDPDMPIAQ-EEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRAL 313
|
....
gi 1744921533 437 QFIA 440
Cdd:cd06534 314 RVAE 317
|
|
| MaoC_like |
cd03446 |
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ... |
530-672 |
1.83e-37 |
|
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.
Pssm-ID: 239530 [Multi-domain] Cd Length: 140 Bit Score: 136.28 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 530 YFEELQPGDSLLTPRRTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGV--GPVIANY 607
Cdd:cd03446 1 YFEDFEIGQVFESVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRLGVfeRTVVAFY 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1744921533 608 GLENLRFIEPVKPGDTIQVRLTCKRKTLKkqrsaEEKPTGVVEWAVEVFNQHQTPVALYSILTLV 672
Cdd:cd03446 81 GIDNLRFLNPVFIGDTIRAEAEVVEKEEK-----DGEDAGVVTRRIEVVNQRGEVVQSGEMSLLV 140
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
7-440 |
2.16e-37 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 145.92 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 7 FLSGTWQSG-RGRSRLIHHAISGEALWEVTSEGLD-----MAAARLFAIEKGAPALRAMtfiERAAMLKAVAKHLLSEKE 80
Cdd:cd07119 1 YIDGEWVEAaSGKTRDIINPANGEVIATVPEGTAEdakraIAAARRAFDSGEWPHLPAQ---ERAALLFRIADKIREDAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 81 RFYAL-SAQTGATRADSWVDIEGGIGTLFTYASLgsrelpddtlwpedelipLSKEGGFAARHVLTSKS-------GVAV 152
Cdd:cd07119 78 ELARLeTLNTGKTLRESEIDIDDVANCFRYYAGL------------------ATKETGEVYDVPPHVISrtvrepvGVCG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 153 HINAFNFP----CWgmleKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHLDSQ--- 225
Cdd:cd07119 140 LITPWNYPllqaAW----KLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGL-PAGVVNLVTGSGATVGAELAESpdv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 226 DVVTFTGSAATGQ---------MLRV-------QPNIVAKSIPFtmeadslnccvlgeDITPDQPEFALFIRevvremtt 289
Cdd:cd07119 215 DLVSFTGGTATGRsimraaagnVKKValelggkNPNIVFADADF--------------ETAVDQALNGVFFN-------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 290 kAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQA--- 366
Cdd:cd07119 273 -AGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRptg 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1744921533 367 DLSAAGAFFPPTLLY-CpqpDETPAVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIA 440
Cdd:cd07119 352 DELAKGYFVEPTIFDdV---DRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVAR 423
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
27-416 |
3.97e-37 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 144.80 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFY-ALSAQTGATRADSWVDIEGGIg 105
Cdd:cd07145 8 NGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAkLLTIEVGKPIKQSRVEVERTI- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 106 TLFTYASLGSRELpddtlwpEDELIPLSKEGGFAARHVLTSKS--GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPA 183
Cdd:cd07145 87 RLFKLAAEEAKVL-------RGETIPVDAYEYNERRIAFTVREpiGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 184 TATAqLTQAMVKSIVDSGLVPEGAISLICGSA---GD-LLDHlDSQDVVTFTGSAATGQmlrvqpNIVAKSIP----FTM 255
Cdd:cd07145 160 SNTP-LTAIELAKILEEAGLPPGVINVVTGYGsevGDeIVTN-PKVNMISFTGSTAVGL------LIASKAGGtgkkVAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 256 EADSLNCCVLGEDITPDQPefalfIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMG 335
Cdd:cd07145 232 ELGGSDPMIVLKDADLERA-----VSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 336 ALVNAEQRADVQEKVNTLLAAGCEIRLGGQADlsaAGAFFPPTLLYCPQPDEtpAVHATEAFGPVATLMPAQNQQHALQL 415
Cdd:cd07145 307 PLISPEAVERMENLVNDAVEKGGKILYGGKRD---EGSFFPPTVLENDTPDM--IVMKEEVFGPVLPIAKVKDDEEAVEI 381
|
.
gi 1744921533 416 A 416
Cdd:cd07145 382 A 382
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
27-416 |
5.62e-37 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 144.11 E-value: 5.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTGATRADSWVDIEGGIG 105
Cdd:cd07103 6 TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLlTLEQGKPLAEARGEVDYAAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 106 TLFTYASLGSRElpddtlwpEDELIPLSkeggFAARHVLTSKS--GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPA 183
Cdd:cd07103 86 FLEWFAEEARRI--------YGRTIPSP----APGKRILVIKQpvGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 184 TATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHL-DSQDV--VTFTGSAATGQMLRVQpniVAKSI-PFTMEads 259
Cdd:cd07103 154 EETPLSALALAELAEEAGL-PAGVLNVVTGSPAEIGEALcASPRVrkISFTGSTAVGKLLMAQ---AADTVkRVSLE--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 260 lnccvLG--------EDITPDQpefalfireVVRE-MTTK---AGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDP 327
Cdd:cd07103 227 -----LGgnapfivfDDADLDK---------AVDGaIASKfrnAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 328 AQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLLyCPQPDETPAVHaTEAFGPVATLMPAQ 407
Cdd:cd07103 293 LDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKR-LGLGGYFYEPTVL-TDVTDDMLIMN-EETFGPVAPIIPFD 369
|
....*....
gi 1744921533 408 NQQHALQLA 416
Cdd:cd07103 370 TEDEVIARA 378
|
|
| MaoC_dehydratas |
pfam01575 |
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ... |
536-652 |
6.44e-37 |
|
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.
Pssm-ID: 396243 [Multi-domain] Cd Length: 123 Bit Score: 134.00 E-value: 6.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 536 PGDSLLT-PRRTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGVGPVIANYGLENLRF 614
Cdd:pfam01575 6 PGEPPDTeKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKVRF 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 1744921533 615 IEPVKPGDTIQVRLTCKRKTLKKQRSAEEKPTGVVEWA 652
Cdd:pfam01575 86 TKPVFPGDTLRTEAEVVGKRDGRQTKVVEVTVEVTEVA 123
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
54-445 |
3.00e-35 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 138.82 E-value: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 54 PALRAMTFIERAAMLKAVAKHLLSEKERF-YALSAQTGATRADSWVDIEGGIGTLFTYASLGSRelpddtlwPEDELIPL 132
Cdd:cd07104 14 KAWAATPPQERAAILRKAAEILEERRDEIaDWLIRESGSTRPKAAFEVGAAIAILREAAGLPRR--------PEGEILPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 133 SKEGGF--AARHVLtsksGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLVPEGAISL 210
Cdd:cd07104 86 DVPGKEsmVRRVPL----GVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIFEEAGLPKGVLNV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 211 ICGSAGDLLDHLDSQ---DVVTFTGSAATGQMLRVqpnIVAKSI-PFTMEADSLNCCVLGEDITPDQP----EFALFIRE 282
Cdd:cd07104 162 VPGGGSEIGDALVEHprvRMISFTGSTAVGRHIGE---LAGRHLkKVALELGGNNPLIVLDDADLDLAvsaaAFGAFLHQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 283 vvremttkaGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRL 362
Cdd:cd07104 239 ---------GQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 363 GGQADlsaaGAFFPPTLLycpqPDETP--AVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFiA 440
Cdd:cd07104 310 GGTYE----GLFYQPTVL----SDVTPdmPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAF-A 380
|
....*
gi 1744921533 441 DAART 445
Cdd:cd07104 381 ERLET 385
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
21-440 |
2.76e-34 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 136.33 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 21 LIHHAISGEALWEVTSEGLDmAAARLFAIEKGAPAlrAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTGATRADSWVD 99
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEE-ALREALALAASYRS--TLTRYQRSAILNKAAALLEARREEFARLiTLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 100 IEGGIGTLFTYASLGSRElpddtlwpEDELIPLSKEGGFAARHVLTSKS--GVAVHINAFNFPCWGMLEKLAPTWLGGMP 177
Cdd:cd07146 79 VGRAADVLRFAAAEALRD--------DGESFSCDLTANGKARKIFTLREplGVVLAITPFNHPLNQVAHKIAPAIAANNR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 178 AIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHLDSQ---DVVTFTGSAATGqmlrvqpNIVAKSIPFT 254
Cdd:cd07146 151 IVLKPSEKTPLSAIYLADLLYEAGL-PPDMLSVVTGEPGEIGDELITHpdvDLVTFTGGVAVG-------KAIAATAGYK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 255 MEADSLNccvlGED--ITPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGV 332
Cdd:cd07146 223 RQLLELG----GNDplIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPAT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 333 KMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADlsaaGAFFPPTLLYCPQPDETPAVHatEAFGPVATLMPAQNQQHA 412
Cdd:cd07146 299 DMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQRQ----GALYAPTVLDHVPPDAELVTE--ETFGPVAPVIRVKDLDEA 372
|
410 420
....*....|....*....|....*...
gi 1744921533 413 LQLACAGGGSLAGTLVTADPQIARQFIA 440
Cdd:cd07146 373 IAISNSTAYGLSSGVCTNDLDTIKRLVE 400
|
|
| R_hydratase_like |
cd03441 |
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ... |
542-663 |
3.67e-34 |
|
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.
Pssm-ID: 239525 [Multi-domain] Cd Length: 127 Bit Score: 126.61 E-value: 3.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 542 TPRRTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGVGPVIANYGLENLRFIEPVKPG 621
Cdd:cd03441 5 SSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGANLGSQSVRFLAPVFPG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1744921533 622 DTIQVRLTCKRKTlkkqrsaEEKPTGVVEWAVEVFNQHQTPV 663
Cdd:cd03441 85 DTLRVEVEVLGKR-------PSKGRGVVTVRTEARNQGGEVV 119
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
3-451 |
4.24e-34 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 136.16 E-value: 4.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 3 QLASFLSGTWQSGRGRSRLIHHAISGEALWEV---TSEGLDMAAARLFAIEKGApaLRAMTFIERAAMLKAVAKHLLSEK 79
Cdd:cd07082 1 QFKYLINGEWKESSGKTIEVYSPIDGEVIGSVpalSALEILEAAETAYDAGRGW--WPTMPLEERIDCLHKFADLLKENK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 80 ERFYA-LSAQTGATRADSWVDIEGGIgTLFTYASLGSRELPDDTLWPEDELIPLSKEGgfaarHVLTSKSGVAVHINAFN 158
Cdd:cd07082 79 EEVANlLMWEIGKTLKDALKEVDRTI-DYIRDTIEELKRLDGDSLPGDWFPGTKGKIA-----QVRREPLGVVLAIGPFN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 159 FPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHL---DSQDVVTFTGSAA 235
Cdd:cd07082 153 YPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGF-PKGVVNVVTGRGREIGDPLvthGRIDVISFTGSTE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 236 TGQMLRVQpnivAKSIPFTMEADSLNCCVLGEDItpdqpEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDAL 315
Cdd:cd07082 232 VGNRLKKQ----HPMKRLVLELGGKDPAIVLPDA-----DLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 316 VARLQKVVVGDPAQEGVKMGALVNaEQRAD-VQEKVNTLLAAGCEIRLGGQADlsaAGAFFPPTLLYCPQPDETpaVHAT 394
Cdd:cd07082 303 KEEVAKLKVGMPWDNGVDITPLID-PKSADfVEGLIDDAVAKGATVLNGGGRE---GGNLIYPTLLDPVTPDMR--LAWE 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1744921533 395 EAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQfIADAARThGRIQI 451
Cdd:cd07082 377 EPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARK-LADALEV-GTVNI 431
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
149-442 |
3.27e-33 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 133.46 E-value: 3.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPC--WGMleKLAPTWLGGMPAIIKPATATAQLTQAMVKsIVDSGL----VPEGAISLICGSA--GDLLD 220
Cdd:cd07086 135 GVVGVITAFNFPVavPGW--NAAIALVCGNTVVWKPSETTPLTAIAVTK-ILAEVLekngLPPGVVNLVTGGGdgGELLV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 221 HLDSQDVVTFTGSAATGQmlRVQPnIVAKsiPFTMEADSL---NCCVLGEDitpdqPEFALFIREVVREMTTKAGQKCTA 297
Cdd:cd07086 212 HDPRVPLVSFTGSTEVGR--RVGE-TVAR--RFGRVLLELggnNAIIVMDD-----ADLDLAVRAVLFAAVGTAGQRCTT 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 298 IRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGG-QADLSAAGAFFP 376
Cdd:cd07086 282 TRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGkRIDGGEPGNYVE 361
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1744921533 377 PTlLYCPQPDETPAVHaTEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIADA 442
Cdd:cd07086 362 PT-IVTGVTDDARIVQ-EETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPK 425
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
63-437 |
7.11e-33 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 132.37 E-value: 7.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 63 ERAAMLKAVAKHLLSEKERFYALS-AQTGATRA---DSWVDieGGIGTLFTYASLGSRELpddtlWPEDeLIPLSKEGGF 138
Cdd:cd07089 43 ERARCLRQLHEALEARKEELRALLvAEVGAPVMtarAMQVD--GPIGHLRYFADLADSFP-----WEFD-LPVPALRGGP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 139 AARHVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAqLTQAMVKSIVDSGLVPEGAISLICGS---A 215
Cdd:cd07089 115 GRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTP-LSALLLGEIIAETDLPAGVVNVVTGSdnaV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 216 GDLLDHLDSQDVVTFTGSAATGQMlrvqpnIVAKSipftmeADSLNCCVL-----GEDITPDQPEFALFIREVVREMTTK 290
Cdd:cd07089 194 GEALTTDPRVDMVSFTGSTAVGRR------IMAQA------AATLKRVLLelggkSANIVLDDADLAAAAPAAVGVCMHN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 291 AGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQ--ADL 368
Cdd:cd07089 262 AGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGrpAGL 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1744921533 369 sAAGAFFPPTLLYCPQPDETpaVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQ----IARQ 437
Cdd:cd07089 342 -DKGFYVEPTLFADVDNDMR--IAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDrayrVARR 411
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
5-438 |
3.78e-32 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 130.58 E-value: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 5 ASFLSGTWQSGRGRSRL-IHHAISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFY 83
Cdd:PLN02278 26 QGLIGGKWTDAYDGKTFpVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 84 AL-SAQTGATRADSWVDIEGGIGTLFTYASLGSRelpddtlwPEDELIPLSkeggFAARHVLTSKS--GVAVHINAFNFP 160
Cdd:PLN02278 106 QLmTLEQGKPLKEAIGEVAYGASFLEYFAEEAKR--------VYGDIIPSP----FPDRRLLVLKQpvGVVGAITPWNFP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 161 CWGMLEKLAPTWLGGMPAIIKPATATAqLTQAMVKSIVDSGLVPEGAISLICGSAGDLLDHLDSQDVV---TFTGSAATG 237
Cdd:PLN02278 174 LAMITRKVGPALAAGCTVVVKPSELTP-LTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVrkiTFTGSTAVG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 238 QMLRVQPNIVAKSIpfTMEADSLNCCVLGEDITPDQPefalfireVVREMTTK---AGQKCTAIRRIIVPQALVNAVSDA 314
Cdd:PLN02278 253 KKLMAGAAATVKRV--SLELGGNAPFIVFDDADLDVA--------VKGALASKfrnSGQTCVCANRILVQEGIYDKFAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 315 LVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLLYCPQPDEtpAVHAT 394
Cdd:PLN02278 323 FSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKR-HSLGGTFYEPTVLGDVTEDM--LIFRE 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1744921533 395 EAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQF 438
Cdd:PLN02278 400 EVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRV 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-440 |
3.83e-32 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 129.96 E-value: 3.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 28 GEALWEV---TSEGLDMA--AARlfaieKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTGATRADSWVDIE 101
Cdd:cd07106 7 GEVFASApvaSEAQLDQAvaAAK-----AAFPGWSATPLEERRAALLAIADAIEANAEELARLlTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 102 GGIGTLFTYASLgsrELPDdtlwpedELIPLSKEGGFAARHV-LtsksGVAVHINAFNFPCWGMLEKLAPTWLGGMPAII 180
Cdd:cd07106 82 GAVAWLRYTASL---DLPD-------EVIEDDDTRRVELRRKpL----GVVAAIVPWNFPLLLAAWKIAPALLAGNTVVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 181 KPATATAQLTQAMVKSIvdSGLVPEGAISLICGSaGDLLDHLDSQ---DVVTFTGSAATGQmlRVQPNiVAKSI-PFTME 256
Cdd:cd07106 148 KPSPFTPLCTLKLGELA--QEVLPPGVLNVVSGG-DELGPALTSHpdiRKISFTGSTATGK--KVMAS-AAKTLkRVTLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 257 ADSLNCCVLGEDITPDqpefalfirEVVREMTTKA----GQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGV 332
Cdd:cd07106 222 LGGNDAAIVLPDVDID---------AVAPKLFWGAfinsGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 333 KMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLLYCPqPDETPAVhATEAFGPVATLMPAQNQQHA 412
Cdd:cd07106 293 TLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEP-LDGPGYFIPPTIVDDP-PEGSRIV-DEEQFGPVLPVLKYSDEDEV 369
|
410 420 430
....*....|....*....|....*....|..
gi 1744921533 413 LQLACAGGGSLAGTLVTADPQ----IARQFIA 440
Cdd:cd07106 370 IARANDSEYGLGASVWSSDLEraeaVARRLEA 401
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
27-416 |
7.56e-32 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 129.29 E-value: 7.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLlseKERF----YALSAQTGATRADSWVDIEG 102
Cdd:cd07147 8 TGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARL---EERFeelaETIVLEAGKPIKDARGEVAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 103 GIGTlFTYASLGSRElpddtlwPEDELIPLSKEGGFAARHVLTSK--SGVAVHINAFNFPCWGMLEKLAPTWLGGMPAII 180
Cdd:cd07147 85 AIDT-FRIAAEEATR-------IYGEVLPLDISARGEGRQGLVRRfpIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 181 KPATATAqLTQAMVKSIVDSGLVPEGAISLI-CGSAG-DLLDHLDSQDVVTFTGSAATGQMLRvqpNIVAKSiPFTMEAD 258
Cdd:cd07147 157 KPASRTP-LSALILGEVLAETGLPKGAFSVLpCSRDDaDLLVTDERIKLLSFTGSPAVGWDLK---ARAGKK-KVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 259 SLNCCVLGEDItpdqpEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALV 338
Cdd:cd07147 232 GNAAVIVDSDA-----DLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 339 NAEQRADVQEKVNTLLAAGCEIRLGGQADlsaaGAFFPPTLLycpqpDETP---AVHATEAFGPVATLMPAQNQQHALQL 415
Cdd:cd07147 307 SESEAERVEGWVNEAVDAGAKLLTGGKRD----GALLEPTIL-----EDVPpdmEVNCEEVFGPVVTVEPYDDFDEALAA 377
|
.
gi 1744921533 416 A 416
Cdd:cd07147 378 V 378
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
42-438 |
7.66e-32 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 128.99 E-value: 7.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 42 AAARLFaiekgaPALRAMTFIERAAMLKAVAKHLLSEKERFY-ALSAQTGATRADSWVDIEGGIGTLFTYASLGSRelpd 120
Cdd:cd07150 29 AAYDAF------PAWAATTPSERERILLKAAEIMERRADDLIdLLIDEGGSTYGKAWFETTFTPELLRAAAGECRR---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 121 dtlwPEDELIPLSKEGGF--AARHVLtsksGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQlTQAMVKSIV 198
Cdd:cd07150 99 ----VRGETLPSDSPGTVsmSVRRPL----GVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV-IGLKIAEIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 199 DSGLVPEGAISLICGSAGDLLDHL-DSQDV--VTFTGSAATGQMLRVqpnIVAKSI-PFTMEADSLNCCVLGEDITPDQP 274
Cdd:cd07150 170 EEAGLPKGVFNVVTGGGAEVGDELvDDPRVrmVTFTGSTAVGREIAE---KAGRHLkKITLELGGKNPLIVLADADLDYA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 275 efalfIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLL 354
Cdd:cd07150 247 -----VRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 355 AAGCEIRLGGQADlsaaGAFFPPTLLYCPQPDETpaVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQI 434
Cdd:cd07150 322 AKGAKLLTGGKYD----GNFYQPTVLTDVTPDMR--IFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQR 395
|
....
gi 1744921533 435 ARQF 438
Cdd:cd07150 396 AFKL 399
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
48-441 |
1.53e-31 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 127.58 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 48 AIEKGA---PALRAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTGATRADSWVDIEGGIGTLFTYASLGSRELPDDtl 123
Cdd:cd07100 4 ALDRAHaafLAWRKTSFAERAALLRKLADLLRERKDELARLiTLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 124 wpedeliPLSKEGGFAarHVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLv 203
Cdd:cd07100 82 -------PIETDAGKA--YVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGF- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 204 PEGAISLICGSAGDLLDHLDSQDV--VTFTGSAATGQmlrvqpnIVAKsipftMEADSLNCCVL---GED--ITPDQPEF 276
Cdd:cd07100 152 PEGVFQNLLIDSDQVEAIIADPRVrgVTLTGSERAGR-------AVAA-----EAGKNLKKSVLelgGSDpfIVLDDADL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 277 ALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAA 356
Cdd:cd07100 220 DKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 357 GCEIRLGGQAdLSAAGAFFPPTLLycpqPDETP--AVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQI 434
Cdd:cd07100 300 GATLLLGGKR-PDGPGAFYPPTVL----TDVTPgmPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLER 374
|
....*..
gi 1744921533 435 ARQFIAD 441
Cdd:cd07100 375 AERVARR 381
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
42-445 |
4.16e-31 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 126.97 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 42 AAARLfAIEKGAPALRAmtfIERAAMLKAVAKHLLSEKERFYALSAQ-TGATRADSWVDIEGGIGTLFTYASLGsrelpd 120
Cdd:cd07109 26 QAARR-AFESGWLRLSP---AERGRLLLRIARLIREHADELARLESLdTGKPLTQARADVEAAARYFEYYGGAA------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 121 DTLwpEDELIPLskEGGFaarHVLTSKS--GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATaTAQLTQAMVKSIV 198
Cdd:cd07109 96 DKL--HGETIPL--GPGY---FVYTVREphGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAE-DAPLTALRLAELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 199 DSGLVPEGAISLICG---SAGDLLDHLDSQDVVTFTGSAATGQmlRVQPNIVAKSIPFTMEADSLNCCVLGEDITPDQpe 275
Cdd:cd07109 168 EEAGLPAGALNVVTGlgaEAGAALVAHPGVDHISFTGSVETGI--AVMRAAAENVVPVTLELGGKSPQIVFADADLEA-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 276 falFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGdPAQEGVKMGALVNAEQRADVQEKVNTLLA 355
Cdd:cd07109 244 ---ALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 356 AGCEIRLGGQA--DLSAAGAFFPPTLLYCPQPDETPAvhATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADpq 433
Cdd:cd07109 320 RGARIVAGGRIaeGAPAGGYFVAPTLLDDVPPDSRLA--QEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD-- 395
|
410
....*....|...
gi 1744921533 434 IARQF-IADAART 445
Cdd:cd07109 396 GDRALrVARRLRA 408
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
24-451 |
9.96e-30 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 122.83 E-value: 9.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 24 HAISGEALWEVTSEGLDMA--AARLfAIEKGaPALRaMTFIERAAMLKAVAKHLLSEKERF-YALSAQTGATRADSWVDI 100
Cdd:cd07118 6 HGVVVARYAEGTVEDVDAAvaAARK-AFDKG-PWPR-MSGAERAAVLLKVADLIRARRERLaLIETLESGKPISQARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 101 EGGIGtLFTYASLGSRELPDDTLwpeDELiplskeGGFAARHVLTSKSGVAVHINAFNFPCWGMLEKLaPTWLG-GMPAI 179
Cdd:cd07118 83 EGAAD-LWRYAASLARTLHGDSY---NNL------GDDMLGLVLREPIGVVGIITPWNFPFLILSQKL-PFALAaGCTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 180 IKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHLDSQ---DVVTFTGSAATGQMlrvqpniVAKSIPFTME 256
Cdd:cd07118 152 VKPSEFTSGTTLMLAELLIEAGL-PAGVVNIVTGYGATVGQAMTEHpdvDMVSFTGSTRVGKA-------IAAAAARNLK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 257 ADSLNccvLG----EDITPDQpEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGV 332
Cdd:cd07118 224 KVSLE---LGgknpQIVFADA-DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPET 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 333 KMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLSAAGAFFPPTLLYCPQPDETPAvhATEAFGPVATLMPAQNQQHA 412
Cdd:cd07118 300 KVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIA--REEIFGPVLSVLTFDTVDEA 377
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1744921533 413 LQLACAGGGSLAGTLVTADPQIArqfIADAARTH-GRIQI 451
Cdd:cd07118 378 IALANDTVYGLSAGVWSKDIDTA---LTVARRIRaGTVWV 414
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
58-455 |
1.46e-29 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 122.41 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 58 AMTFIERAAMLKAVAKHLLSEKERF-YALSAQTGATRADSWVDIEGGIGTLFTYASLGSRelpddtlwPEDELIPLSKEG 136
Cdd:cd07151 50 ATLPQERAEILEKAAQILEERRDEIvEWLIRESGSTRIKANIEWGAAMAITREAATFPLR--------MEGRILPSDVPG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 137 gfAARHVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLVPEGAISLICGSAG 216
Cdd:cd07151 122 --KENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 217 DLLDHLDSQ---DVVTFTGSAATGQML-RVQPNIVAKSipfTMEADSLNCCVLGEDITPDQP-EFALFIRevvremTTKA 291
Cdd:cd07151 200 EIGDAFVEHpvpRLISFTGSTPVGRHIgELAGRHLKKV---ALELGGNNPFVVLEDADIDAAvNAAVFGK------FLHQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 292 GQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADlsaa 371
Cdd:cd07151 271 GQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAE---- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 372 GAFFPPTLLyCPQPDETPAVHaTEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFI--ADAARTHGRI 449
Cdd:cd07151 347 GNVLEPTVL-SDVTNDMEIAR-EEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFArrIDAGMTHIND 424
|
....*.
gi 1744921533 450 QILNEE 455
Cdd:cd07151 425 QPVNDE 430
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-416 |
4.26e-29 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 120.89 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 28 GEALWEV---TSEGLDMAAArlfAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTG----ATRADswvD 99
Cdd:cd07092 7 GEEIATVpdaSAADVDAAVA---AAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALeSRNTGkplhLVRDD---E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 100 IEGGIGTLFTYASlGSRELPDdtlwpedeliplSKEGGFAARHVLTSKS---GVAVHINAFNFPCWGMLEKLAPTWLGGM 176
Cdd:cd07092 81 LPGAVDNFRFFAG-AARTLEG------------PAAGEYLPGHTSMIRRepiGVVAQIAPWNYPLMMAAWKIAPALAAGN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 177 PAIIKPATATAqLTQAMVKSIVDSGLvPEGAISLICG---SAGDLLDHLDSQDVVTFTGSAATG-QMLRVQPNIVAKSI- 251
Cdd:cd07092 148 TVVLKPSETTP-LTTLLLAELAAEVL-PPGVVNVVCGggaSAGDALVAHPRVRMVSLTGSVRTGkKVARAAADTLKRVHl 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 252 ------PFTMEADSlnccvlgeditpDQPEFALFIREVVremTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVG 325
Cdd:cd07092 226 elggkaPVIVFDDA------------DLDAAVAGIATAG---YYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 326 DPAQEGVKMGALVNAEQRADVQEKVnTLLAAGCEIRLGGQAdLSAAGAFFPPTLLY-CPQPDEtpaVHATEAFGPVATLM 404
Cdd:cd07092 291 DPDDEDTEMGPLNSAAQRERVAGFV-ERAPAHARVLTGGRR-AEGPGYFYEPTVVAgVAQDDE---IVQEEIFGPVVTVQ 365
|
410
....*....|..
gi 1744921533 405 PAQNQQHALQLA 416
Cdd:cd07092 366 PFDDEDEAIELA 377
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
48-442 |
9.29e-29 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 120.14 E-value: 9.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 48 AIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTGATRADSWVDIEGGIGTLFTYASLGSR--------EL 118
Cdd:cd07131 45 AAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLvTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRlfgetvpsEL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 119 PDDTLwpedeliplskeggFAARHVLtsksGVAVHINAFNFP----CWgmleKLAPTWLGGMPAIIKPATATAQLTQAMV 194
Cdd:cd07131 125 PNKDA--------------MTRRQPI----GVVALITPWNFPvaipSW----KIFPALVCGNTVVFKPAEDTPACALKLV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 195 KSIVDSGLvPEGAISLI---CGSAGD-LLDHLDSqDVVTFTGSAATGQmlRVQpNIVAKSI-PFTMEADSLNCCVLGEDI 269
Cdd:cd07131 183 ELFAEAGL-PPGVVNVVhgrGEEVGEaLVEHPDV-DVVSFTGSTEVGE--RIG-ETCARPNkRVALEMGGKNPIIVMDDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 270 TPDqpefaLFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEK 349
Cdd:cd07131 258 DLD-----LALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 350 VNTLLAAGCEIRLGGQA---DLSAAGAFFPPTLLYCPQPDETpaVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGT 426
Cdd:cd07131 333 NEIGKEEGATLLLGGERltgGGYEKGYFVEPTVFTDVTPDMR--IAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSA 410
|
410
....*....|....*.
gi 1744921533 427 LVTADPQIARQFIADA 442
Cdd:cd07131 411 IYTEDVNKAFRARRDL 426
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
54-416 |
2.23e-28 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 118.81 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 54 PALRAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTGATRADSWVDIEGGIGTLFTYASLGsrelpdDTLwpEDELIPL 132
Cdd:cd07114 35 GAWRKLTPTERGKLLRRLADLIEANAEELAELeTRDNGKLIRETRAQVRYLAEWYRYYAGLA------DKI--EGAVIPV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 133 SKeGGFaarHVLTSKS--GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISL 210
Cdd:cd07114 107 DK-GDY---LNFTRREplGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGF-PPGVVNV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 211 ICG---SAGDLL-DHLDSqDVVTFTGSAATGQmlRVQPNIVAKSIPFTMEadslnccvLG--------EDITPDQPE--- 275
Cdd:cd07114 182 VTGfgpETGEALvEHPLV-AKIAFTGGTETGR--HIARAAAENLAPVTLE--------LGgkspnivfDDADLDAAVngv 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 276 -FALFIrevvremttKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLL 354
Cdd:cd07114 251 vAGIFA---------AAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAR 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1744921533 355 AAGCEIRLGGQA---DLSAAGAFFPPTLLYCPQPDeTPAVHaTEAFGPVATLMPAQNQQHALQLA 416
Cdd:cd07114 322 EEGARVLTGGERpsgADLGAGYFFEPTILADVTND-MRIAQ-EEVFGPVLSVIPFDDEEEAIALA 384
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
7-451 |
2.40e-28 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 118.76 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 7 FLSGTWQSGRGRSRL-IHHAISGEALWEV---TSEGLDMAAArlfAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERF 82
Cdd:cd07138 2 YIDGAWVAPAGTETIdVINPATEEVIGTVplgTAADVDRAVA---AARRAFPAWSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 83 Y-ALSAQTGATRADS-WVDIEGGIGTLFTYASLgSRELPddtlWPEdeliplsKEGGFAARHVltsKSGVAVHINAFNFP 160
Cdd:cd07138 79 AqAITLEMGAPITLArAAQVGLGIGHLRAAADA-LKDFE----FEE-------RRGNSLVVRE---PIGVCGLITPWNWP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 161 CWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGlVPEGAISLICGS---AGDLL-DHLDSqDVVTFTGSAAT 236
Cdd:cd07138 144 LNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAG-LPAGVFNLVNGDgpvVGEALsAHPDV-DMVSFTGSTRA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 237 GQ---------MLRV-------QPNIvaksipftmeadslnccvlgedITPDQpEFALFIREVVREMTTKAGQKCTAIRR 300
Cdd:cd07138 222 GKrvaeaaadtVKRValelggkSANI----------------------ILDDA-DLEKAVPRGVAACFANSGQSCNAPTR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 301 IIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQA--DLSAAGAFFPPT 378
Cdd:cd07138 279 MLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGrpEGLERGYFVKPT 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1744921533 379 LLycpqPDETP--AVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQfIADAARThGRIQI 451
Cdd:cd07138 359 VF----ADVTPdmTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARA-VARRLRA-GQVHI 427
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
7-451 |
1.60e-26 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 113.70 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 7 FLSGTWQSGRGRSRL-IHHAISGEALWEV---TSEGLDMAAArlfAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERF 82
Cdd:cd07117 4 FINGEWVKGSSGETIdSYNPANGETLSEItdaTDADVDRAVK---AAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 83 YALSAQTGAT--RADSWVDIEGGIGTLFTYASLGSRELPDDTLWPEDELiplskeggfaaRHVLTSKSGVAVHINAFNFP 160
Cdd:cd07117 81 AMVETLDNGKpiRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTL-----------SIVLREPIGVVGQIIPWNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 161 CWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDsgLVPEGAISLICG---SAGDLLDHLDSQDVVTFTGSAATG 237
Cdd:cd07117 150 FLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQD--VLPKGVVNIVTGkgsKSGEYLLNHPGLDKLAFTGSTEVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 238 QMlrVQPNIVAKSIPFTMEadslnccvLG---EDITPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDA 314
Cdd:cd07117 228 RD--VAIAAAKKLIPATLE--------LGgksANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 315 LVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQ---ADLSAAGAFFPPTLLycPQPDETPAV 391
Cdd:cd07117 298 LKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHrltENGLDKGFFIEPTLI--VNVTNDMRV 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 392 HATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQfIADAARThGRIQI 451
Cdd:cd07117 376 AQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALR-VARAVET-GRVWV 433
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
36-450 |
2.16e-26 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 112.84 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 36 SEGLDMAAArlfAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYALSA-QTG-ATRADSWVDIEGGIGTLFTYASL 113
Cdd:cd07108 18 AADVDRAVA---AAKAAFPEWAATPARERGKLLARIADALEARSEELARLLAlETGnALRTQARPEAAVLADLFRYFGGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 114 GSrELPDDTLWPEDELIPLSKeggfaaRHVLtsksGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATAtAQLTQAM 193
Cdd:cd07108 95 AG-ELKGETLPFGPDVLTYTV------REPL----GVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED-APLAVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 194 VKSIVdSGLVPEGAISLICGSAGD----LLDHLDSqDVVTFTGSAATGQmlrvqpnIVAKS-----IPFTMEADSLNCCV 264
Cdd:cd07108 163 LAEIL-AQVLPAGVLNVITGYGEEcgaaLVDHPDV-DKVTFTGSTEVGK-------IIYRAaadrlIPVSLELGGKSPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 265 LGEDITPDQpefalFIREVVREMT-TKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQR 343
Cdd:cd07108 234 VFPDADLDD-----AVDGAIAGMRfTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 344 ADVQEKVNTLLAA-GCEIRLGG---QADLSAAGAFFPPTLLycPQPDETPAVHATEAFGPVATLMPAQNQQHALQLACAG 419
Cdd:cd07108 309 AKVCGYIDLGLSTsGATVLRGGplpGEGPLADGFFVQPTIF--SGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDS 386
|
410 420 430
....*....|....*....|....*....|.
gi 1744921533 420 GGSLAGTLVTADpqiarqfIADAARTHGRIQ 450
Cdd:cd07108 387 HYGLAAYVWTRD-------LGRALRAAHALE 410
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
42-468 |
2.19e-26 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 112.36 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 42 AAARlfaieKGAPALRAMTFIERAAMLKAVAKHLLSEKERF-YALSAQTG------ATRADSWV-DIEGGIGTLFTYASL 113
Cdd:cd07095 7 AAAR-----AAFPGWAALSLEERAAILRRFAELLKANKEELaRLISRETGkplweaQTEVAAMAgKIDISIKAYHERTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 114 GSRELPDdtlwpedeliplskeggfaARHVLTSKS-GVAVHINAFNFPcwGMLEK--LAPTWLGGMPAIIKPATATAQLT 190
Cdd:cd07095 82 RATPMAQ-------------------GRAVLRHRPhGVMAVFGPFNFP--GHLPNghIVPALLAGNTVVFKPSELTPAVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 191 QAMVKSIVDSGLvPEGAISLICGSA---GDLLDHlDSQDVVTFTGSAATGQMLRVQ-PNIVAKSIPFTMEADslNCCVLG 266
Cdd:cd07095 141 ELMVELWEEAGL-PPGVLNLVQGGRetgEALAAH-EGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGN--NPLVVW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 267 EDITPDQPefalfIREVVREMTTKAGQKCTAIRRIIVPQ-ALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRAD 345
Cdd:cd07095 217 DVADIDAA-----AYLIVQSAFLTAGQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAAR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 346 VQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLL----YCPQPDEtpavhatEAFGPVATLMPAQNQQHALQLACAGGG 421
Cdd:cd07095 292 YLLAQQDLLALGGEPLLAMER-LVAGTAFLSPGIIdvtdAADVPDE-------EIFGPLLQVYRYDDFDEAIALANATRF 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1744921533 422 SLAGTLVTADPQIARQFiadaaRTHGRIQILNEEsaKESTGHGSPLP 468
Cdd:cd07095 364 GLSAGLLSDDEALFERF-----LARIRAGIVNWN--RPTTGASSTAP 403
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
6-451 |
4.60e-26 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 112.31 E-value: 4.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 6 SFLSGTWQSGR-GRSRLIHHAISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYA 84
Cdd:PRK11241 13 ALINGEWLDANnGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 85 L-SAQTGATRADSWVDIEGGIGTLFTYASLGSReLPDDTL---WPEDELIplskeggfaarhVLTSKSGVAVHINAFNFP 160
Cdd:PRK11241 93 LmTLEQGKPLAEAKGEISYAASFIEWFAEEGKR-IYGDTIpghQADKRLI------------VIKQPIGVTAAITPWNFP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 161 CWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGlVPEGAISLICGSAGDLLDHLDSQDVV---TFTGSAATG 237
Cdd:PRK11241 160 AAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAG-IPAGVFNVVTGSAGAVGGELTSNPLVrklSFTGSTEIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 238 QMLRVQpniVAKSIpftmEADSLNCCVLGEDITPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVA 317
Cdd:PRK11241 239 RQLMEQ---CAKDI----KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 318 RLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADlSAAGAFFPPTLLYcpQPDETPAVHATEAF 397
Cdd:PRK11241 312 AVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAH-ELGGNFFQPTILV--DVPANAKVAKEETF 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1744921533 398 GPVATLMPAQNQQHALQLACAGGGSLAGTLVTADpqIARQFIADAARTHGRIQI 451
Cdd:PRK11241 389 GPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD--LSRVFRVGEALEYGIVGI 440
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
54-431 |
4.61e-26 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 111.89 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 54 PALRAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTGATRAD-SWVDIEGGIGTLFTYASLgSRELPDDTLWPEDELIp 131
Cdd:cd07093 33 PGWSRMSPAERARILHKVADLIEARADELALLeSLDTGKPITLaRTRDIPRAAANFRFFADY-ILQLDGESYPQDGGAL- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 132 lskeggfaaRHVLTSKSGVAVHINAFNFPCwgMLE--KLAPTWLGGMPAIIKPATATAqLTQAMVKSIVDSGLVPEGAIS 209
Cdd:cd07093 111 ---------NYVLRQPVGVAGLITPWNLPL--MLLtwKIAPALAFGNTVVLKPSEWTP-LTAWLLAELANEAGLPPGVVN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 210 LICG---SAGDLL-DHLDSqDVVTFTGSAATGQmlRVQPNIVAKSIPFTMEADSLNCCVLGEDITPDQPefalfIREVVR 285
Cdd:cd07093 179 VVHGfgpEAGAALvAHPDV-DLISFTGETATGR--TIMRAAAPNLKPVSLELGGKNPNIVFADADLDRA-----VDAAVR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 286 EMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGG- 364
Cdd:cd07093 251 SSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGg 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1744921533 365 --QADLSAAGAFFPPTLLYcpQPDETPAVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTAD 431
Cdd:cd07093 331 rpELPDLEGGYFVEPTVIT--GLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
27-440 |
9.78e-26 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 110.99 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVT---SEGLDMAAArlfAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYALSAQ-TGAT-RADSWVDIE 101
Cdd:cd07115 6 TGELIARVAqasAEDVDAAVA---AARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLdTGKPiRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 102 GGIGTLFTYASLGSRElpddtlwpEDELIPLSkegGFAARHVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIK 181
Cdd:cd07115 83 RAADTFRYYAGWADKI--------EGEVIPVR---GPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 182 PATATAQLTQAMVKSIVDSGlVPEGAISLICG---SAGD-LLDHLDSqDVVTFTGSAATGQML---------RVQPNIVA 248
Cdd:cd07115 152 PAELTPLSALRIAELMAEAG-FPAGVLNVVTGfgeVAGAaLVEHPDV-DKITFTGSTAVGRKImqgaagnlkRVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 249 KSIPFTMEADSLNCCVLGEditpdqpEFALFIrevvremttKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPA 328
Cdd:cd07115 230 KSANIVFADADLDAAVRAA-------ATGIFY---------NQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 329 QEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADlSAAGAFFPPTLLYCPQPDETpaVHATEAFGPVATLMPAQN 408
Cdd:cd07115 294 DPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGKRP-GARGFFVEPTIFAAVPPEMR--IAQEEIFGPVVSVMRFRD 370
|
410 420 430
....*....|....*....|....*....|..
gi 1744921533 409 QQHALQLACAGGGSLAGTLVTADPQIARQFIA 440
Cdd:cd07115 371 EEEALRIANGTEYGLAAGVWTRDLGRAHRVAA 402
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
126-416 |
2.83e-25 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 108.67 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 126 EDELIPLSKEGgfaaRHVLTSKS--GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLv 203
Cdd:PRK10090 52 EGEIIQSDRPG----ENILLFKRalGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGL- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 204 PEGAISLICGSA---GDLLDHLDSQDVVTFTGSAATGQ--MLRVQPNIVAKSIPFTMEADSLNCcvlgeditpDQPEFAL 278
Cdd:PRK10090 127 PKGVFNLVLGRGetvGQELAGNPKVAMVSMTGSVSAGEkiMAAAAKNITKVCLELGGKAPAIVM---------DDADLDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 279 FIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEG-VKMGALVNAEQRADVQEKVNTLLAAG 357
Cdd:PRK10090 198 AVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEG 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1744921533 358 CEIRLGGQADlSAAGAFFPPTLLYcpQPDETPAVHATEAFGPVATLMPAQNQQHALQLA 416
Cdd:PRK10090 278 ARVALGGKAV-EGKGYYYPPTLLL--DVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMA 333
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
26-450 |
3.07e-25 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 109.61 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 26 ISGEALWEVTSEGLD-----MAAARLfAIEKGAPALRAMTfiERAAMLKAVAKHLLSEKERFYAL-SAQTGATRADSW-V 98
Cdd:cd07112 10 ATGRVLAEVAACDAAdvdraVAAARR-AFESGVWSRLSPA--ERKAVLLRLADLIEAHRDELALLeTLDMGKPISDALaV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 99 DIEGGIGTLFTYAslgsrELPDDTLwpeDELIPlskeggfAARHVLTSKS----GVAVHINAFNFPCWGMLEKLAPTWLG 174
Cdd:cd07112 87 DVPSAANTFRWYA-----EAIDKVY---GEVAP-------TGPDALALITreplGVVGAVVPWNFPLLMAAWKIAPALAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 175 GMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICG---SAGDLLDHLDSQDVVTFTGSAATGQML----------R 241
Cdd:cd07112 152 GNSVVLKPAEQSPLTALRLAELALEAGL-PAGVLNVVPGfghTAGEALGLHMDVDALAFTGSTEVGRRFleysgqsnlkR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 242 V-------QPNIVAksipftmeadslnccvlgeditPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDA 314
Cdd:cd07112 231 VwlecggkSPNIVF----------------------ADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 315 LVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLSAAGAFF-PPTLLYCPQPDETpaVHA 393
Cdd:cd07112 289 VVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTETGGFFvEPTVFDGVTPDMR--IAR 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1744921533 394 TEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADpqiarqfIADAARTHGRIQ 450
Cdd:cd07112 367 EEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSD-------LSRAHRVARRLR 416
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
27-441 |
4.20e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 109.06 E-value: 4.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYAL-SAQTGATRADSWVDIEGGIG 105
Cdd:PRK09406 10 TGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALmTLEMGKTLASAKAEALKCAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 106 TLFTYASLGSRELPDDtlwPEDeliplSKEGGFAARHVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATA 185
Cdd:PRK09406 90 GFRYYAEHAEALLADE---PAD-----AAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 186 TAQlTQAMVKSIVDSGLVPEGAISLICGSAGDLLDHLDSQDVV--TFTGSAATGQMlrvqpniVAksipfTMEADSLNCC 263
Cdd:PRK09406 162 VPQ-TALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAaaTLTGSEPAGRA-------VA-----AIAGDEIKKT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 264 VL---GED--ITPDQPEFALFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALV 338
Cdd:PRK09406 229 VLelgGSDpfIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 339 NAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLLycpqPDETP--AVHATEAFGPVATLMPAQNQQHALQLA 416
Cdd:PRK09406 309 TEQGRDEVEKQVDDAVAAGATILCGGKR-PDGPGWFYPPTVI----TDITPdmRLYTEEVFGPVASLYRVADIDEAIEIA 383
|
410 420
....*....|....*....|....*
gi 1744921533 417 CAGGGSLAGTLVTADPQIARQFIAD 441
Cdd:PRK09406 384 NATTFGLGSNAWTRDEAEQERFIDD 408
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
7-451 |
6.07e-25 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 108.97 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 7 FLSGTWQSG-RGRSRLIHHAISGEALWEV---TSEGLDMAaarLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERF 82
Cdd:cd07559 4 FINGEWVAPsKGEYFDNYNPVNGKVLCEIprsTAEDVDLA---VDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 83 -YALSAQTG-ATRADSWVDIEGGIGTLFTYASL------GSRELPDDTLwpedeliplskeggfaaRHVLTSKSGVAVHI 154
Cdd:cd07559 81 aVAETLDNGkPIRETLAADIPLAIDHFRYFAGViraqegSLSEIDEDTL-----------------SYHFHEPLGVVGQI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 155 NAFNFP----CWgmleKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDsgLVPEGAISLICG---SAGDLLDHLDSQDV 227
Cdd:cd07559 144 IPWNFPllmaAW----KLAPALAAGNTVVLKPASQTPLSILVLMELIGD--LLPKGVVNVVTGfgsEAGKPLASHPRIAK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 228 VTFTGSAATGQ--MLRVQPNIvaksIPFTME--ADSLNccVLGEDITPDQPEFALFIREVVREMTTKAGQKCTAIRRIIV 303
Cdd:cd07559 218 LAFTGSTTVGRliMQYAAENL----IPVTLElgGKSPN--IFFDDAMDADDDFDDKAEEGQLGFAFNQGEVCTCPSRALV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 304 PQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLS---AAGAFFPPTLL 380
Cdd:cd07559 292 QESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLgglDKGYFYEPTLI 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1744921533 381 YCPQPDETpaVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADpqIARQF-IADAARThGRIQI 451
Cdd:cd07559 372 KGGNNDMR--IFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRD--INRALrVARGIQT-GRVWV 438
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
27-440 |
1.14e-24 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 107.78 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAkHLLSEKERFYAL--SAQTGATRADSWVDIEGGI 104
Cdd:cd07090 6 TGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAA-DLLRERNDEIARleTIDNGKPIEEARVDIDSSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 105 GTLFTYASLGSrelpddTLwpEDELIPLSkEGGFA--ARHVLtsksGVAVHINAFNFP----CWgmleKLAPTWLGGMPA 178
Cdd:cd07090 85 DCLEYYAGLAP------TL--SGEHVPLP-GGSFAytRREPL----GVCAGIGAWNYPiqiaSW----KSAPALACGNAM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 179 IIKPATATAqLTQAMVKSIVDSGLVPEGAISLICGSA--GDLLDHLDSQDVVTFTGSAATGQmlRVQPNIVAKSIPFTME 256
Cdd:cd07090 148 VYKPSPFTP-LTALLLAEILTEAGLPDGVFNVVQGGGetGQLLCEHPDVAKVSFTGSVPTGK--KVMSAAAKGIKHVTLE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 257 ADSLNCCVLGEDITPDQpefALFIREVVREMTTkaGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGA 336
Cdd:cd07090 225 LGGKSPLIIFDDADLEN---AVNGAMMANFLSQ--GQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 337 LVNAEQRADVQEKVNTLLAAGCEIRLGGQ----ADLSAAGAFFPPTLLYCPQPDETpaVHATEAFGPVATLMPAQNQQHA 412
Cdd:cd07090 300 LISEEHLEKVLGYIESAKQEGAKVLCGGErvvpEDGLENGFYVSPCVLTDCTDDMT--IVREEIFGPVMSILPFDTEEEV 377
|
410 420
....*....|....*....|....*...
gi 1744921533 413 LQLACAGGGSLAGTLVTADPQIARQFIA 440
Cdd:cd07090 378 IRRANDTTYGLAAGVFTRDLQRAHRVIA 405
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
28-431 |
1.30e-24 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 107.38 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 28 GEALWEV---TSEGLDMAAARLFAIEkgaPALRAMTFIERAAMLKAVAKHLLSEKERFY-ALSAQTGATRADSWVDIEGG 103
Cdd:cd07152 1 GAVLGEVgvaDAADVDRAAARAAAAQ---RAWAATPPRERAAVLRRAADLLEEHADEIAdWIVRESGSIRPKAGFEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 104 IGTLFTYASLGSRelpddtlwPEDELIPLSKEGGFAARHVLTSKSGVavhINAFNFPCWGMLEKLAPTWLGGMPAIIKPA 183
Cdd:cd07152 78 IGELHEAAGLPTQ--------PQGEILPSAPGRLSLARRVPLGVVGV---ISPFNFPLILAMRSVAPALALGNAVVLKPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 184 TATAQLTQAMVKSIVDSGLVPEGAISLICG--SAGDLLDHLDSQDVVTFTGSAATGQMLRVQPNIVAKSIpfTMEADSLN 261
Cdd:cd07152 147 PRTPVSGGVVIARLFEEAGLPAGVLHVLPGgaDAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKV--SLELGGKN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 262 CCVLGEDITPDQP----EFALFIREvvremttkaGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGAL 337
Cdd:cd07152 225 ALIVLDDADLDLAasngAWGAFLHQ---------GQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 338 VNAEQRADVQEKVNTLLAAGCEIRLGGQADlsaaGAFFPPTLLYCPQPDEtpAVHATEAFGPVATLMPAQNQQHALQLAC 417
Cdd:cd07152 296 INARQLDRVHAIVDDSVAAGARLEAGGTYD----GLFYRPTVLSGVKPGM--PAFDEEIFGPVAPVTVFDSDEEAVALAN 369
|
410
....*....|....
gi 1744921533 418 AGGGSLAGTLVTAD 431
Cdd:cd07152 370 DTEYGLSAGIISRD 383
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
10-416 |
2.07e-24 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 107.69 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 10 GTWQSGRGRSRLIHHAISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLlseKERFYALSA-- 87
Cdd:cd07124 39 GKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALL---RRRRFELAAwm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 88 --QTGATRADSWVDIEGGIGTLFTYAslgsRELPDdtLWPEdeliPLSKEGGFAARHVLTSKsGVAVHINAFNFPC---W 162
Cdd:cd07124 116 vlEVGKNWAEADADVAEAIDFLEYYA----REMLR--LRGF----PVEMVPGEDNRYVYRPL-GVGAVISPWNFPLailA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 163 GMLekLAPTwLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGS---AGD-LLDHLDSqDVVTFTGSAATGQ 238
Cdd:cd07124 185 GMT--TAAL-VTGNTVVLKPAEDTPVIAAKLVEILEEAGL-PPGVVNFLPGPgeeVGDyLVEHPDV-RFIAFTGSREVGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 239 ML-----RVQPNIV-AKsiPFTMEADSLNCCVLGEDITPDQPefalfIREVVREMTTKAGQKCTAIRRIIVPQALVNAVS 312
Cdd:cd07124 260 RIyeraaKVQPGQKwLK--RVIAEMGGKNAIIVDEDADLDEA-----AEGIVRSAFGFQGQKCSACSRVIVHESVYDEFL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 313 DALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGcEIRLGGQADLSAAGAFF-PPTLLYCPQPDETPAv 391
Cdd:cd07124 333 ERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAEGYFvQPTIFADVPPDHRLA- 410
|
410 420
....*....|....*....|....*
gi 1744921533 392 hATEAFGPVATLMPAQNQQHALQLA 416
Cdd:cd07124 411 -QEEIFGPVLAVIKAKDFDEALEIA 434
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
149-441 |
2.11e-24 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 106.87 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHLDSQDV- 227
Cdd:PRK13968 128 GTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGI-PQGVYGWLNADNDGVSQMINDSRIa 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 228 -VTFTGSAATGQMLRVQPnivaksipftmeADSLNCCVL---GED--ITPDQPEFALFIREVVREMTTKAGQKCTAIRRI 301
Cdd:PRK13968 207 aVTVTGSVRAGAAIGAQA------------GAALKKCVLelgGSDpfIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRF 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 302 IVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQaDLSAAGAFFPPTLLy 381
Cdd:PRK13968 275 IIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGE-KIAGAGNYYAPTVL- 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1744921533 382 cpqPDETPAVHA--TEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIAD 441
Cdd:PRK13968 353 ---ANVTPEMTAfrEELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAAR 411
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-447 |
2.83e-24 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 106.54 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 28 GEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYA-LSAQTGATRADSWVDIEGGIGT 106
Cdd:cd07099 6 GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAElLHAETGKPRADAGLEVLLALEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 107 LFTYASLGSRELPDDTLWPedeliplskeGGFAARHVLTSKS---GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPA 183
Cdd:cd07099 86 IDWAARNAPRVLAPRKVPT----------GLLMPNKKATVEYrpyGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 184 TATAqLTQAMVKSIVDSGLVPEGAISLICGSAG---DLLDHldSQDVVTFTGSAATGQmlRVQPNIVAKSIPFTMEADSL 260
Cdd:cd07099 156 EVTP-LVGELLAEAWAAAGPPQGVLQVVTGDGAtgaALIDA--GVDKVAFTGSVATGR--KVMAAAAERLIPVVLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 261 NCCVLGEDITPDQPEFAlfireVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNA 340
Cdd:cd07099 231 DPMIVLADADLERAAAA-----AVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 341 EQRADVQEKVNTLLAAGCEIRLGGqADLSAAGAFFPPTLLYCPqPDETPAVHAtEAFGPVATLMPAQNQQHALQLACAGG 420
Cdd:cd07099 306 RQLDIVRRHVDDAVAKGAKALTGG-ARSNGGGPFYEPTVLTDV-PHDMDVMRE-ETFGPVLPVMPVADEDEAIALANDSR 382
|
410 420 430
....*....|....*....|....*....|....*..
gi 1744921533 421 GSLAGTLVTADP----QIARQF------IADAARTHG 447
Cdd:cd07099 383 YGLSASVFSRDLaraeAIARRLeagavsINDVLLTAG 419
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
63-400 |
4.11e-24 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 105.96 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 63 ERAAMLKAVAKHLLSEKERFYALSAQTGAT-RADSWVDIEGGIGTLFTYA----SLGSRELPDDtlwpedeLIPLSkegg 137
Cdd:cd07148 45 ERIAILERLADLMEERADELALLIAREGGKpLVDAKVEVTRAIDGVELAAdelgQLGGREIPMG-------LTPAS---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 138 fAARHVLTSKS--GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLVPEGAISLICGSA 215
Cdd:cd07148 114 -AGRIAFTTREpiGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 216 GDLLDHLDSQ-DVVTFTGSAATGQMLRvqpnivAKSIPFTMeadslncCVLGED-----ITPDQPEFALFIREVVREMTT 289
Cdd:cd07148 193 VAEKLVTDPRvAFFSFIGSARVGWMLR------SKLAPGTR-------CALEHGgaapvIVDRSADLDAMIPPLVKGGFY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 290 KAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIrLGGQADLS 369
Cdd:cd07148 260 HAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARL-LCGGKRLS 338
|
330 340 350
....*....|....*....|....*....|.
gi 1744921533 370 AagAFFPPTLLYCPQPDETPAVHatEAFGPV 400
Cdd:cd07148 339 D--TTYAPTVLLDPPRDAKVSTQ--EIFGPV 365
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
149-439 |
4.68e-24 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 106.14 E-value: 4.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPC--WGMLEKLAPTwlGGMPAIIKPATAT---AQLTQAMVKSIVDSGLVPEGAISLICGSA--GDLLDH 221
Cdd:cd07130 134 GVVGVITAFNFPVavWGWNAAIALV--CGNVVVWKPSPTTpltAIAVTKIVARVLEKNGLPGAIASLVCGGAdvGEALVK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 222 LDSQDVVTFTGSAATGQmlRVQPNIVA---KSIpftMEADSLNCCVLGEDitpdqPEFALFIREVVREMTTKAGQKCTAI 298
Cdd:cd07130 212 DPRVPLVSFTGSTAVGR--QVGQAVAArfgRSL---LELGGNNAIIVMED-----ADLDLAVRAVLFAAVGTAGQRCTTT 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 299 RRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPT 378
Cdd:cd07130 282 RRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKV-IDGPGNYVEPT 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1744921533 379 LLYCPQPDetPAVHaTEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFI 439
Cdd:cd07130 361 IVEGLSDA--PIVK-EETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWL 418
|
|
| FkbR2 |
cd03451 |
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ... |
530-664 |
8.58e-24 |
|
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved family of proteins found in prokaryotes and archaea but not in eukaryotes. FkbR2 has sequence similarity to (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The function of FkbR2 is unknown.
Pssm-ID: 239535 [Multi-domain] Cd Length: 146 Bit Score: 97.66 E-value: 8.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 530 YFEELQPGDSLL-TPRRTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGVGPVIANYG 608
Cdd:cd03451 3 YFEDFTVGQVFEhAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSLTAVANLG 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1744921533 609 LENLRFIEPVKPGDTIQVRLTCkrktLKKQRSAEEKPTGVVEWAVEVFNQHQTPVA 664
Cdd:cd03451 83 YDEVRFPAPVFHGDTLYAESEV----LSKRESKSRPDAGIVTVRTVGYNQDGEPVL 134
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
149-416 |
1.03e-23 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 105.22 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFP----CWgmleKLAPTWLGGMPAIIKPaTATAQLTQAMVKSIVDSGLVPEGAISLICGS---AGDLLDH 221
Cdd:cd07113 144 GVVAGIVPWNFSvmiaVW----KIGAALATGCTIVIKP-SEFTPLTLLRVAELAKEAGIPDGVLNVVNGKgavGAQLISH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 222 LDSQDVvTFTGSAATGQMLRVQPniVAKSIPFTMEADSLNCCVLGEDITPDQpefalFIREVVREMTTKAGQKCTAIRRI 301
Cdd:cd07113 219 PDVAKV-SFTGSVATGKKIGRQA--ASDLTRVTLELGGKNAAAFLKDADIDW-----VVEGLLTAGFLHQGQVCAAPERF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 302 IVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLLY 381
Cdd:cd07113 291 YVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEA-LAGEGYFVQPTLVL 369
|
250 260 270
....*....|....*....|....*....|....*
gi 1744921533 382 CPQPDETpaVHATEAFGPVATLMPAQNQQHALQLA 416
Cdd:cd07113 370 ARSADSR--LMREETFGPVVSFVPYEDEEELIQLI 402
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
26-440 |
1.47e-23 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 104.25 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 26 ISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFY-ALSAQTGATRADSWVDIEGGI 104
Cdd:cd07102 4 IDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAeELTWQMGRPIAQAGGEIRGML 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 105 GTLFTYASLGSRELPDdtlwpedelIPLSKEGGFAaRHVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPAT 184
Cdd:cd07102 84 ERARYMISIAEEALAD---------IRVPEKDGFE-RYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 185 ATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHLDSQDV--VTFTGSAATGQmlRVQPNIVAKSIPFTMEadslnc 262
Cdd:cd07102 154 QTPLCGERFAAAFAEAGL-PEGVFQVLHLSHETSAALIADPRIdhVSFTGSVAGGR--AIQRAAAGRFIKVGLE------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 263 cvLG-ED---ITPD-QPEFALFirEVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGAL 337
Cdd:cd07102 225 --LGgKDpayVRPDaDLDAAAE--SLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 338 VNAEQRADVQEKVNTLLAAGCEIRLGGQ--ADLSAAGAFFPPTLLycPQPDETPAVHATEAFGPVATLMPAQNQQHALQL 415
Cdd:cd07102 301 VSARAADFVRAQIADAIAKGARALIDGAlfPEDKAGGAYLAPTVL--TNVDHSMRVMREETFGPVVGIMKVKSDAEAIAL 378
|
410 420
....*....|....*....|....*
gi 1744921533 416 ACAGGGSLAGTLVTADPQIARQFIA 440
Cdd:cd07102 379 MNDSEYGLTASVWTKDIARAEALGE 403
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-416 |
2.53e-23 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 103.84 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 7 FLSGTWQSGRGRSRLIHHAISGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYAL- 85
Cdd:PRK13473 6 LINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 86 SAQTG----ATRADswvDIEGGIGTLFTYA--------SLGSRELPDDTLWPEDELIplskeggfaarhvltsksGVAVH 153
Cdd:PRK13473 86 SLNCGkplhLALND---EIPAIVDVFRFFAgaarclegKAAGEYLEGHTSMIRRDPV------------------GVVAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 154 INAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAqLTQAMVKSIVdSGLVPEGAISLICG---SAGD-LLDHLDSqDVVT 229
Cdd:PRK13473 145 IAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITP-LTALKLAELA-ADILPPGVLNVVTGrgaTVGDaLVGHPKV-RMVS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 230 FTGSAATGQmlrvqpNIV---AKSIPFT-MEadslnccvLG--------EDITPDQpefalfireVVREMTT----KAGQ 293
Cdd:PRK13473 222 LTGSIATGK------HVLsaaADSVKRThLE--------LGgkapvivfDDADLDA---------VVEGIRTfgyyNAGQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 294 KCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLSAAGA 373
Cdd:PRK13473 279 DCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGY 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1744921533 374 FFPPTLLY-CPQPDEtpaVHATEAFGPVATLMPAQNQQHALQLA 416
Cdd:PRK13473 359 YYEPTLLAgARQDDE---IVQREVFGPVVSVTPFDDEDQAVRWA 399
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
35-433 |
2.36e-22 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 100.96 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 35 TSEGLDMA--AAR-LFAIEKGAPALRAmTFIERAAMLKAVAKHLLSEKERFYALSAQTGATRAD--SWvDIEGGIGTLFT 109
Cdd:PLN02467 43 TAEDVDAAveAARkAFKRNKGKDWART-TGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDeaAW-DMDDVAGCFEY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 110 YASLGSR---------ELPDDTlwpedeliplskeggFAArHVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAII 180
Cdd:PLN02467 121 YADLAEAldakqkapvSLPMET---------------FKG-YVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 181 KPaTATAQLTQAMVKSIVDSGLVPEGAISLICG---SAGDLLDHLDSQDVVTFTGSAATGQ--MLRVQPNIVaksiPFTM 255
Cdd:PLN02467 185 KP-SELASVTCLELADICREVGLPPGVLNVVTGlgtEAGAPLASHPGVDKIAFTGSTATGRkiMTAAAQMVK----PVSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 256 EADSLNCCVLGEDITPDQP-EFALFirevvrEMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKM 334
Cdd:PLN02467 260 ELGGKSPIIVFDDVDLDKAvEWAMF------GCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 335 GALVNAEQRADVQEKVNTLLAAGCEIRLGGQA-DLSAAGAFFPPTLLYCPQPDETpaVHATEAFGPVATLMPAQNQQHAL 413
Cdd:PLN02467 334 GPVVSEGQYEKVLKFISTAKSEGATILCGGKRpEHLKKGFFIEPTIITDVTTSMQ--IWREEVFGPVLCVKTFSTEDEAI 411
|
410 420
....*....|....*....|
gi 1744921533 414 QLACAGGGSLAGTLVTADPQ 433
Cdd:PLN02467 412 ELANDSHYGLAGAVISNDLE 431
|
|
| R_hydratase |
cd03449 |
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ... |
534-639 |
6.13e-22 |
|
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.
Pssm-ID: 239533 [Multi-domain] Cd Length: 128 Bit Score: 91.84 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 534 LQPGDSLlTPRRTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGVGP-VIAnygLE-N 611
Cdd:cd03449 1 LKVGDSA-SLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPgTIY---LSqS 76
|
90 100
....*....|....*....|....*...
gi 1744921533 612 LRFIEPVKPGDTIQVRLTCKRKTLKKQR 639
Cdd:cd03449 77 LRFLRPVFIGDTVTATVTVTEKREDKKR 104
|
|
| YdeM |
cd03454 |
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ... |
531-664 |
5.73e-21 |
|
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown function. YdeM has sequence similarity to the hot-dog fold of (R)-specific enoyl-CoA hydratase. Other enzymes with this fold include the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.
Pssm-ID: 239538 [Multi-domain] Cd Length: 140 Bit Score: 89.55 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 531 FEELQPGDSLLTPRRTMTEADIVNFAClsgdHF---YAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDAGVG--PVIA 605
Cdd:cd03454 1 FEDLVIGQRFTSGSYTVTEEEIIAFAR----EFdpqPFHLDEEAAKESLFGGLAASGWHTAAITMRLLVDAGLSgsASGG 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1744921533 606 NYGLENLRFIEPVKPGDTIQVRLTCkrktLKKQRSAEEKPTGVVEWAVEVFNQHQTPVA 664
Cdd:cd03454 77 SPGIDELRWPRPVRPGDTLSVEVEV----LDKRPSRSRPDRGIVTLRSETLNQRGEVVL 131
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
4-416 |
6.28e-21 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 96.31 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 4 LASFLSGTWQSGRGRSRL-IHHAISGEALWEVT-SEGLDMAAArLFAIEKGAPALRAMTFIERAAMLKAVAKHLlSEKER 81
Cdd:cd07111 22 FGHFINGKWVKPENRKSFpTINPATGEVLASVLqAEEEDVDAA-VAAARTAFESWSALPGHVRARHLYRIARHI-QKHQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 82 FYAL--SAQTG-ATRADSWVDIEGGIGTLFTYASlgsrelpddtlWPEdeliplSKEGGFAARHVLtsksGVAVHINAFN 158
Cdd:cd07111 100 LFAVleSLDNGkPIRESRDCDIPLVARHFYHHAG-----------WAQ------LLDTELAGWKPV----GVVGQIVPWN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 159 FPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAG---DLLDHLDSqDVVTFTGSAA 235
Cdd:cd07111 159 FPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGL-PPGVLNIVTGNGSfgsALANHPGV-DKVAFTGSTE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 236 TGQMLRVQPNIVAKSIPFTMEADSLNccVLGEDITPDQPefalfIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDAL 315
Cdd:cd07111 237 VGRALRRATAGTGKKLSLELGGKSPF--IVFDDADLDSA-----VEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 316 VARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGqADLSAAGAFFPPTLLYCPQPdeTPAVHATE 395
Cdd:cd07111 310 KERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPG-ADLPSKGPFYPPTLFTNVPP--ASRIAQEE 386
|
410 420
....*....|....*....|.
gi 1744921533 396 AFGPVATLMPAQNQQHALQLA 416
Cdd:cd07111 387 IFGPVLVVLTFRTAKEAVALA 407
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
149-439 |
6.81e-21 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 96.44 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVK---SIVDSGLVPEGAISLICGSA--GDLLDHLD 223
Cdd:PLN02315 156 GIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKlvaEVLEKNNLPGAIFTSFCGGAeiGEAIAKDT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 224 SQDVVTFTGSAATGQMlrVQPNIVAKSIPFTMEADSLNCCVLGEDitpdqPEFALFIREVVREMTTKAGQKCTAIRRIIV 303
Cdd:PLN02315 236 RIPLVSFTGSSKVGLM--VQQTVNARFGKCLLELSGNNAIIVMDD-----ADIQLAVRSVLFAAVGTAGQRCTTCRRLLL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 304 PQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLLycp 383
Cdd:PLN02315 309 HESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSA-IESEGNFVQPTIV--- 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1744921533 384 QPDETPAVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFI 439
Cdd:PLN02315 385 EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWI 440
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
149-445 |
7.30e-21 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 96.22 E-value: 7.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHL-DSQDV 227
Cdd:cd07101 120 GVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGL-PRDLWQVVTGPGSEVGGAIvDNADY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 228 VTFTGSAATGQmlRVQPNIVAKSIPFTMEADSLNCCVLGEDITPDQPEfalfiREVVREMTTKAGQKCTAIRRIIVPQAL 307
Cdd:cd07101 199 VMFTGSTATGR--VVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAA-----AGAVRACFSNAGQLCVSIERIYVHESV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 308 VNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLSAAGAFFPPTLLycPQPDE 387
Cdd:cd07101 272 YDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGPYFYEPTVL--TGVTE 349
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1744921533 388 TPAVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQfIADAART 445
Cdd:cd07101 350 DMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRR-IAARLRA 406
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
27-450 |
2.62e-20 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 94.36 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYALSA-QTGATRADSWVDIEGGIG 105
Cdd:cd07107 6 TGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDAlDCGNPVSAMLGDVMVAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 106 TLFTYASLGSrELPDDTlwpedelIPLSKEGGFAARHvltSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPAtA 185
Cdd:cd07107 86 LLDYFAGLVT-ELKGET-------IPVGGRNLHYTLR---EPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPP-E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 186 TAQLTQAMVKSIVDsGLVPEGAISLICGS---AGD-LLDHLDSqDVVTFTGSAATGQMLRVQpniVAKSI-PFTMEADSL 260
Cdd:cd07107 154 QAPLSALRLAELAR-EVLPPGVFNILPGDgatAGAaLVRHPDV-KRIALIGSVPTGRAIMRA---AAEGIkHVTLELGGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 261 NCCVLGEDITPDQpefalFIREVVREMT-TKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVN 339
Cdd:cd07107 229 NALIVFPDADPEA-----AADAAVAGMNfTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 340 AEQRADVQEKVNTLLAAGCEIRLGG---QADLSAAGAFFPPTLLycpqPDETP--AVHATEAFGPVATLMPAQNQQHALQ 414
Cdd:cd07107 304 RQQYDRVMHYIDSAKREGARLVTGGgrpEGPALEGGFYVEPTVF----ADVTPgmRIAREEIFGPVLSVLRWRDEAEMVA 379
|
410 420 430
....*....|....*....|....*....|....*.
gi 1744921533 415 LACAGGGSLAGTLVTADpqiarqfIADAARTHGRIQ 450
Cdd:cd07107 380 QANGVEYGLTAAIWTND-------ISQAHRTARRVE 408
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
149-441 |
6.37e-20 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 93.13 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVkSIVDSGLVPEGA----ISLICGsAGDLLDHLDS 224
Cdd:cd07098 122 GVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFL-SIIRECLAACGHdpdlVQLVTC-LPETAEALTS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 225 Q---DVVTFTGSAATGQMlrvqpniVAKSipftmEADSLNCCVL---GED---ITPDQpEFALFIREVVREMTTKAGQKC 295
Cdd:cd07098 200 HpviDHITFIGSPPVGKK-------VMAA-----AAESLTPVVLelgGKDpaiVLDDA-DLDQIASIIMRGTFQSSGQNC 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 296 TAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGG---QADLSAAG 372
Cdd:cd07098 267 IGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGkryPHPEYPQG 346
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1744921533 373 AFFPPTLLYcpqpDETP--AVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIAD 441
Cdd:cd07098 347 HYFPPTLLV----DVTPdmKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQ 413
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1-404 |
1.46e-19 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 92.64 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 1 MQQLASFLSGTWQ-----SGRGRSRLIHHAIS-----GEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKA 70
Cdd:cd07125 20 ADALKAFDEKEWEaipiiNGEETETGEGAPVIdpadhERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 71 VAkHLLSE-KERF-YALSAQTGATRADSWVDIEGGIGTLFTYASLGSRELPDDTL-WPEDELIPLSKEGgfaarhvltsk 147
Cdd:cd07125 100 AA-DLLEAnRGELiALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELpGPTGELNGLELHG----------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 148 SGVAVHINAFNFP----CWGMLEKLAptwlGGMPAIIKPATATAQLTQAMVKSIVDSGlVPEGAISLICGSAGDLLDHLD 223
Cdd:cd07125 168 RGVFVCISPWNFPlaifTGQIAAALA----AGNTVIAKPAEQTPLIAARAVELLHEAG-VPRDVLQLVPGDGEEIGEALV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 224 SQ---DVVTFTGSAATGQ-MLRVQPNIVAKSIPFTMEADSLNCCVLgeDITPDqPEFAlfIREVVREMTTKAGQKCTAIR 299
Cdd:cd07125 243 AHpriDGVIFTGSTETAKlINRALAERDGPILPLIAETGGKNAMIV--DSTAL-PEQA--VKDVVQSAFGSAGQRCSALR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 300 RIIVpqalVNAVSDALVARLQKVV----VGDPAQEGVKMGALVNAEQRAdvqekvntLLAAGCEI-----RLGGQADLSA 370
Cdd:cd07125 318 LLYL----QEEIAERFIEMLKGAMaslkVGDPWDLSTDVGPLIDKPAGK--------LLRAHTELmrgeaWLIAPAPLDD 385
|
410 420 430
....*....|....*....|....*....|....*
gi 1744921533 371 A-GAFFPPTLLYcpqpDETPAVHATEAFGPVATLM 404
Cdd:cd07125 386 GnGYFVAPGIIE----IVGIFDLTTEVFGPILHVI 416
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
170-416 |
8.22e-19 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 90.32 E-value: 8.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 170 PTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHL-DSQDVVTFTGSAATGQMLRVQpniVA 248
Cdd:PRK09407 177 PALLAGNAVVLKPDSQTPLTALAAVELLYEAGL-PRDLWQVVTGPGPVVGTALvDNADYLMFTGSTATGRVLAEQ---AG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 249 KS-IPFTMEADSLNCCVLGEDITPDQPefalfIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDP 327
Cdd:PRK09407 253 RRlIGFSLELGGKNPMIVLDDADLDKA-----AAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAG 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 328 AQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQA--DLSAagAFFPPTLLYCPQPDETpaVHATEAFGPVATLMP 405
Cdd:PRK09407 328 YDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKArpDLGP--LFYEPTVLTGVTPDME--LAREETFGPVVSVYP 403
|
250
....*....|.
gi 1744921533 406 AQNQQHALQLA 416
Cdd:PRK09407 404 VADVDEAVERA 414
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
42-416 |
3.14e-18 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 87.63 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 42 AAARLFaiekgaPALRAMTFIERAAMLKAVAKHLLSEKERFYALS-AQTGATRADSWVDIEGGIGTLFTYASLGSRelpd 120
Cdd:cd07105 8 AAAAAF------PAWSKTPPSERRDILLKAADLLESRRDEFIEAMmEETGATAAWAGFNVDLAAGMLREAASLITQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 121 dtlwPEDELIPLSKEGGFAarhvLTSKS--GVAVHINAFNfpcwgmleklAPTWLGG----MP------AIIKPATATAQ 188
Cdd:cd07105 78 ----IIGGSIPSDKPGTLA----MVVKEpvGVVLGIAPWN----------APVILGTraiaYPlaagntVVLKASELSPR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 189 LTQAMVKSIVDSGLvPEGAISLICGSAGD-------LLDHldsQDV--VTFTGSAATGqmlRVQPNIVAKSI-PFTMEAD 258
Cdd:cd07105 140 THWLIGRVFHEAGL-PKGVLNVVTHSPEDapevveaLIAH---PAVrkVNFTGSTRVG---RIIAETAAKHLkPVLLELG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 259 SLNCCVLGEDITpdqpefalfIREVVREMTTKA----GQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDpaqegVKM 334
Cdd:cd07105 213 GKAPAIVLEDAD---------LDAAANAALFGAflnsGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 335 GALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLSAAGAFFPPTLLYCPQPDEtpAVHATEAFGPVATLMPAQNQQHALQ 414
Cdd:cd07105 279 GSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGTSMPPTILDNVTPDM--DIYSEESFGPVVSIIRVKDEEEAVR 356
|
..
gi 1744921533 415 LA 416
Cdd:cd07105 357 IA 358
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
34-400 |
4.89e-18 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 87.66 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 34 VTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYALSAQ-TGATRADSWVDIEGGIGTLFTYAS 112
Cdd:TIGR01238 68 VFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVReAGKTIHNAIAEVREAVDFCRYYAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 113 LGSRELPDDTLWPEdeliplskeggfaarhvltsksGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQA 192
Cdd:TIGR01238 148 QVRDVLGEFSVESR----------------------GVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 193 MVKSIVDSGlVPEGAISLICGSAGDLLDHLDSQDV---VTFTGSAATGQmlRVQPNIVAK---SIPFTMEADSLNCCVLG 266
Cdd:TIGR01238 206 AVELMQEAG-FPAGTIQLLPGRGADVGAALTSDPRiagVAFTGSTEVAQ--LINQTLAQRedaPVPLIAETGGQNAMIVD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 267 EDITPDQpefalFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADV 346
Cdd:TIGR01238 283 STALPEQ-----VVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNL 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1744921533 347 QEKVNTLLAAGCEIRLGGQADLSAA--GAFFPPTLLYCPQPDETpavhATEAFGPV 400
Cdd:TIGR01238 358 LAHIEHMSQTQKKIAQLTLDDSRACqhGTFVAPTLFELDDIAEL----SEEVFGPV 409
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
7-468 |
1.24e-17 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 86.17 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 7 FLSGTWQSGRGRSRLIHHAISGEALWE---VTSEGLDMA--AARlfaieKGAPALRAMTFIERAAMLKAVAKHLLSEKER 81
Cdd:PRK09457 4 WINGDWIAGQGEAFESRNPVSGEVLWQgndATAAQVDAAvrAAR-----AAFPAWARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 82 FYALSAQ-TG------ATRADSWVD-IEGGIGTLFTYASLGSRELPDdtlwpedeliplskeggfaARHVLTSKS-GVAV 152
Cdd:PRK09457 79 LAEVIAReTGkplweaATEVTAMINkIAISIQAYHERTGEKRSEMAD-------------------GAAVLRHRPhGVVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 153 HINAFNFPcwGMLEK--LAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSA--GDLLDHLDSQDVV 228
Cdd:PRK09457 140 VFGPYNFP--GHLPNghIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGL-PAGVLNLVQGGRetGKALAAHPDIDGL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 229 TFTGSAATGQMLRVQ----PNIVaksipFTMEADSLNCCVLGEdiTPDQPEFALFIrevVREMTTKAGQKCTAIRRIIVP 304
Cdd:PRK09457 217 LFTGSANTGYLLHRQfagqPEKI-----LALEMGGNNPLVIDE--VADIDAAVHLI---IQSAFISAGQRCTCARRLLVP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 305 QAlvnAVSDALVARLQKVV----VGDP-AQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTL 379
Cdd:PRK09457 287 QG---AQGDAFLARLVAVAkrltVGRWdAEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQ-LQAGTGLLTPGI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 380 L----YCPQPDEtpavhatEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIAdaartHGRIQILNEE 455
Cdd:PRK09457 363 IdvtgVAELPDE-------EYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLL-----EIRAGIVNWN 430
|
490
....*....|...
gi 1744921533 456 saKESTGHGSPLP 468
Cdd:PRK09457 431 --KPLTGASSAAP 441
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
149-416 |
1.81e-17 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 85.71 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHLDSQD-- 226
Cdd:cd07083 156 GAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGF-PPGVVQFLPGVGEEVGAYLTEHEri 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 227 -VVTFTGSAATGQMLRVQPNIVAKS----IPFTMEADSLNCCVLGEDITPDQpefalFIREVVREMTTKAGQKCTAIRRI 301
Cdd:cd07083 235 rGINFTGSLETGKKIYEAAARLAPGqtwfKRLYVETGGKNAIIVDETADFEL-----VVEGVVVSAFGFQGQKCSAASRL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 302 IVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGcEIRLGGQADlSAAGAFFPPTLLY 381
Cdd:cd07083 310 ILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRL-EGEGYFVAPTVVE 387
|
250 260 270
....*....|....*....|....*....|....*..
gi 1744921533 382 CPQPDETpaVHATEAFGPVATLM--PAQNQQHALQLA 416
Cdd:cd07083 388 EVPPKAR--IAQEEIFGPVLSVIryKDDDFAEALEVA 422
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
27-436 |
3.39e-17 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 84.93 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAML-KAVAkhLLSEKERFYAL--SAQTGA----TRAdswVD 99
Cdd:PRK13252 31 TGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILrRAVD--ILRERNDELAAleTLDTGKpiqeTSV---VD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 100 IEGGIGTLFTYASLGSrelpddTLwpEDELIPLsKEGGFA--ARHVLtsksGVAVHINAFNFP----CWgmleKLAPTWL 173
Cdd:PRK13252 106 IVTGADVLEYYAGLAP------AL--EGEQIPL-RGGSFVytRREPL----GVCAGIGAWNYPiqiaCW----KSAPALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 174 GGMPAIIKPATATAqLTQAMVKSIVDSGLVPEGAISLICGSA--GDLLDHLDSQDVVTFTGSAATGQmlRVQPNIVAKSI 251
Cdd:PRK13252 169 AGNAMIFKPSEVTP-LTALKLAEIYTEAGLPDGVFNVVQGDGrvGAWLTEHPDIAKVSFTGGVPTGK--KVMAAAAASLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 252 PFTMEadslnccvLG--------EDITPDqpefalfiREVVREMTTK---AGQKCTAIRRIIVPQALVNAVSDALVARLQ 320
Cdd:PRK13252 246 EVTME--------LGgksplivfDDADLD--------RAADIAMLANfysSGQVCTNGTRVFVQKSIKAAFEARLLERVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 321 KVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQA---DLSAAGAFFPPTLLY-CpqPDETPAVHaTEA 396
Cdd:PRK13252 310 RIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERlteGGFANGAFVAPTVFTdC--TDDMTIVR-EEI 386
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1744921533 397 FGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADpqIAR 436
Cdd:PRK13252 387 FGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTAD--LSR 424
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
149-431 |
6.81e-17 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 84.12 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICG---SAGDLL-DHLDS 224
Cdd:cd07143 146 GVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGF-PPGVINVVSGygrTCGNAIsSHMDI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 225 qDVVTFTGSAATGQM-LRVQPNIVAKSIPFTMEADSLNccVLGEDITPDQP----EFALFIREvvremttkaGQKCTAIR 299
Cdd:cd07143 225 -DKVAFTGSTLVGRKvMEAAAKSNLKKVTLELGGKSPN--IVFDDADLESAvvwtAYGIFFNH---------GQVCCAGS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 300 RIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADlSAAGAFFPPTL 379
Cdd:cd07143 293 RIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRH-GNEGYFIEPTI 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1744921533 380 LycpqPDETP--AVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTAD 431
Cdd:cd07143 372 F----TDVTEdmKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNN 421
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
33-431 |
1.53e-16 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 82.64 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 33 EVTSEGLDMA--AARLfAIEKGAPalRAMTFIERAAMLKAVAKHLLSEKERFYALSA-QTGAT-RADSWVDIEGGIGTLF 108
Cdd:cd07091 37 EADEEDVDAAvkAARA-AFETGWW--RKMDPRERGRLLNKLADLIERDRDELAALESlDNGKPlEESAKGDVALSIKCLR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 109 TYASLGsrelpdDTLwpEDELIPLSKEGGFAARHVltsKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQ 188
Cdd:cd07091 114 YYAGWA------DKI--QGKTIPIDGNFLAYTRRE---PIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 189 LTQAMVKSIVDSGLvPEGAISLICGS---AGDLL-DHLDSqDVVTFTGSAATGQMLRVQpniVAKS--IPFTMEADSLNC 262
Cdd:cd07091 183 SALYLAELIKEAGF-PPGVVNIVPGFgptAGAAIsSHMDV-DKIAFTGSTAVGRTIMEA---AAKSnlKKVTLELGGKSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 263 CVLGEDITPDQPEFALFIRevvreMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQ 342
Cdd:cd07091 258 NIVFDDADLDKAVEWAAFG-----IFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 343 RADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLLYCPQPDETPAvhATEAFGPVATLMPAQNQQHALQLACAGGGS 422
Cdd:cd07091 333 FDKILSYIESGKKEGATLLTGGER-HGSKGYFIQPTVFTDVKDDMKIA--KEEIFGPVVTILKFKTEDEVIERANDTEYG 409
|
....*....
gi 1744921533 423 LAGTLVTAD 431
Cdd:cd07091 410 LAAGVFTKD 418
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
27-435 |
3.58e-16 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 81.77 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVT---SEGLDMA--AARlFAIEKGaPALRaMTFIERAAMLKAVAKHLLSEKERFYALSAQTGATRAD--SWVD 99
Cdd:cd07142 28 NGEVIAHVAegdAEDVDRAvkAAR-KAFDEG-PWPR-MTGYERSRILLRFADLLEKHADELAALETWDNGKPYEqaRYAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 100 IEGGIGtLFTYASLGSRELPDDTLwPEDeliplskeGGFAArHVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAI 179
Cdd:cd07142 105 VPLAAR-LFRYYAGWADKIHGMTL-PAD--------GPHHV-YTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 180 IKPATATAQLTQAMVKSIVDSGLvPEGAISLICG----SAGDLLDHLDSqDVVTFTGSAATGqmlRVQPNIVAKS--IPF 253
Cdd:cd07142 174 LKPAEQTPLSALLAAKLAAEAGL-PDGVLNIVTGfgptAGAAIASHMDV-DKVAFTGSTEVG---KIIMQLAAKSnlKPV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 254 TMEADSLNCCVLGEDITPDQ----PEFALFIREvvremttkaGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQ 329
Cdd:cd07142 249 TLELGGKSPFIVCEDADVDKavelAHFALFFNQ---------GQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 330 EGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLLYCPQPDEtpAVHATEAFGPVATLMPAQNQ 409
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDR-IGSKGYYIQPTIFSDVKDDM--KIARDEIFGPVQSILKFKTV 396
|
410 420
....*....|....*....|....*.
gi 1744921533 410 QHALQLACAGGGSLAGTLVTADPQIA 435
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTA 422
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
28-404 |
6.41e-16 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 80.85 E-value: 6.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 28 GEALWEVtSEG----LDMA--AARLfAIEKGAPaLRAMTFIERAAMLKAVAKhlLSEKERFYALSAQTGAT----RADSW 97
Cdd:cd07141 32 GEKICEV-QEGdkadVDKAvkAARA-AFKLGSP-WRTMDASERGRLLNKLAD--LIERDRAYLASLETLDNgkpfSKSYL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 98 VDIEGGIGTLFTYASlgsrelpddtlWPED---ELIPLskEGGFaarHVLTSKSGVAV--HINAFNFPCWGMLEKLAPTW 172
Cdd:cd07141 107 VDLPGAIKVLRYYAG-----------WADKihgKTIPM--DGDF---FTYTRHEPVGVcgQIIPWNFPLLMAAWKLAPAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 173 LGGMPAIIKPATATAqLTQAMVKSIVDSGLVPEGAISLICG---SAGDLL-DHLDSqDVVTFTGSAATGQML-------- 240
Cdd:cd07141 171 ACGNTVVLKPAEQTP-LTALYLASLIKEAGFPPGVVNVVPGygpTAGAAIsSHPDI-DKVAFTGSTEVGKLIqqaagksn 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 241 --RVQPNIVAKSiPFTMEADSlnccvlGEDITPDQPEFALFIrevvremttKAGQKCTAIRRIIVPQALVNAVSDALVAR 318
Cdd:cd07141 249 lkRVTLELGGKS-PNIVFADA------DLDYAVEQAHEALFF---------NMGQCCCAGSRTFVQESIYDEFVKRSVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 319 LQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLLYCPQPDETPAvhATEAFG 398
Cdd:cd07141 313 AKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKR-HGDKGYFIQPTVFSDVTDDMRIA--KEEIFG 389
|
....*.
gi 1744921533 399 PVATLM 404
Cdd:cd07141 390 PVQQIF 395
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
149-416 |
3.52e-15 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 78.82 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSA---GD-LLDHLDS 224
Cdd:PRK03137 173 GVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGL-PAGVVNFVPGSGsevGDyLVDHPKT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 225 QdVVTFTGSAATGQML-----RVQP-NIVAKSIPFTMEA-DSLnccVLGEDItpdqpEFALFIREVVREMTTKAGQKCTA 297
Cdd:PRK03137 252 R-FITFTGSREVGLRIyeraaKVQPgQIWLKRVIAEMGGkDAI---VVDEDA-----DLDLAAESIVASAFGFSGQKCSA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 298 IRRIIVPQALVNAVSDALVARLQKVVVGDPAqEGVKMGALVNAEQradvQEKVNTLLAAGCE---IRLGGQADLSaAGAF 374
Cdd:PRK03137 323 CSRAIVHEDVYDEVLEKVVELTKELTVGNPE-DNAYMGPVINQAS----FDKIMSYIEIGKEegrLVLGGEGDDS-KGYF 396
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1744921533 375 FPPTLLYCPQPDETPAvhATEAFGPVATLMPAQNQQHALQLA 416
Cdd:PRK03137 397 IQPTIFADVDPKARIM--QEEIFGPVVAFIKAKDFDHALEIA 436
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
142-429 |
7.18e-15 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 77.93 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 142 HVLTSKSGVAVHINAFNFP----CWgmleKLAPTWLGGMPAIIKPATATAqLTQAMVKSIVDSGLVPEGAISLICG---S 214
Cdd:PLN02466 190 QTLHEPIGVAGQIIPWNFPllmfAW----KVGPALACGNTIVLKTAEQTP-LSALYAAKLLHEAGLPPGVLNVVSGfgpT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 215 AG-DLLDHLDSqDVVTFTGSAATGQMLRvqpNIVAKS--IPFTMEADSLNCCVLGEDITPDQ----PEFALFIREvvrem 287
Cdd:PLN02466 265 AGaALASHMDV-DKLAFTGSTDTGKIVL---ELAAKSnlKPVTLELGGKSPFIVCEDADVDKavelAHFALFFNQ----- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 288 ttkaGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAd 367
Cdd:PLN02466 336 ----GQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDR- 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1744921533 368 LSAAGAFFPPTLLYCPQPDETPAvhATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVT 429
Cdd:PLN02466 411 FGSKGYYIQPTVFSNVQDDMLIA--QDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFT 470
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
27-435 |
1.08e-14 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 77.17 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 27 SGEALWEVTS---EGLDMA--AARlFAIEKGaPALRaMTFIERAAMLKAVAKHLLSEKERFYALSAQTGAT--RADSWVD 99
Cdd:PLN02766 45 TGEVIARIAEgdkEDVDLAvkAAR-EAFDHG-PWPR-MSGFERGRIMMKFADLIEEHIEELAALDTIDAGKlfALGKAVD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 100 IEGGIGTLFTYASLGSRelpddtlwPEDELIPLSKE-GGFAARHVLtsksGVAVHINAFNFPCWGMLEKLAPTWLGGMPA 178
Cdd:PLN02766 122 IPAAAGLLRYYAGAADK--------IHGETLKMSRQlQGYTLKEPI----GVVGHIIPWNFPSTMFFMKVAPALAAGCTM 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 179 IIKPATATAqLTQAMVKSIVDSGLVPEGAISLICG---SAGDLL-DHLDSqDVVTFTGSAATGQMLrVQPNIVAKSIPFT 254
Cdd:PLN02766 190 VVKPAEQTP-LSALFYAHLAKLAGVPDGVINVVTGfgpTAGAAIaSHMDV-DKVSFTGSTEVGRKI-MQAAATSNLKQVS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 255 MEADSLNCCVLGEDITPDQP-EFALFirevvrEMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVK 333
Cdd:PLN02766 267 LELGGKSPLLIFDDADVDMAvDLALL------GIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 334 MGALVNAEQRADVQEKVNTLLAAGCEIRLGGQAdLSAAGAFFPPTLLYCPQPDETPAvhATEAFGPVATLMPAQNQQHAL 413
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGATLLTGGKP-CGDKGYYIEPTIFTDVTEDMKIA--QDEIFGPVMSLMKFKTVEEAI 417
|
410 420
....*....|....*....|..
gi 1744921533 414 QLACAGGGSLAGTLVTADPQIA 435
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVA 439
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
149-441 |
4.33e-14 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 75.14 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFP----CWgmleKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICG---SAGD-LLD 220
Cdd:cd07144 146 GVCGQIIPWNYPlamaAW----KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGF-PPGVVNIIPGygaVAGSaLAE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 221 HLDSqDVVTFTGSAATGQmlrvqpnIVAKSIPFTMEADSLNC-----CVLGEDITPDQPefalfIREVVREMTTKAGQKC 295
Cdd:cd07144 221 HPDV-DKIAFTGSTATGR-------LVMKAAAQNLKAVTLECggkspALVFEDADLDQA-----VKWAAAGIMYNSGQNC 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 296 TAIRRIIVPQalvnAVSDALVARLQKVV-----VGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQ--ADL 368
Cdd:cd07144 288 TATSRIYVQE----SIYDKFVEKFVEHVkqnykVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEkaPEG 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1744921533 369 SAAGAFFPPTLLY-CPQpdeTPAVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIAD 441
Cdd:cd07144 364 LGKGYFIPPTIFTdVPQ---DMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARE 434
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
144-451 |
1.08e-13 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 74.02 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 144 LTSKS--GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDH 221
Cdd:PLN00412 153 LTSKIplGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGF-PKGLISCVTGKGSEIGDF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 222 LDSQ---DVVTFTGsAATGqmLRVQPNivAKSIPFTMEADSLNCCVLGEDITPDqpefaLFIREVVREMTTKAGQKCTAI 298
Cdd:PLN00412 232 LTMHpgvNCISFTG-GDTG--IAISKK--AGMVPLQMELGGKDACIVLEDADLD-----LAAANIIKGGFSYSGQRCTAV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 299 RRIIVPQALVNAVSDALVARLQKVVVGDPaQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRlggqADLSAAGAFFPPT 378
Cdd:PLN00412 302 KVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFC----QEWKREGNLIWPL 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1744921533 379 LLYCPQPDETPAVHatEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQfIADAARThGRIQI 451
Cdd:PLN00412 377 LLDNVRPDMRIAWE--EPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAIL-ISDAMET-GTVQI 445
|
|
| PRK08190 |
PRK08190 |
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated |
531-633 |
2.06e-13 |
|
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
Pssm-ID: 236180 [Multi-domain] Cd Length: 466 Bit Score: 72.99 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 531 FEELQPGDSLlTPRRTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFV---LSAAAGLfVDAGVGPVianY 607
Cdd:PRK08190 11 FDEIAIGDSA-SLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGgalISAVLGT-RLPGPGTI---Y 85
|
90 100
....*....|....*....|....*.
gi 1744921533 608 GLENLRFIEPVKPGDTIQVRLTCKRK 633
Cdd:PRK08190 86 LGQSLRFRRPVRIGDTLTVTVTVREK 111
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
149-440 |
2.68e-12 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 69.09 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKP---ATATAQLtqamVKSIVDSGLVPEgAISLICGS---AGDLLDHl 222
Cdd:cd07087 102 GVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPselAPATSAL----LAKLIPKYFDPE-AVAVVEGGvevATALLAE- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 223 dSQDVVTFTGSAATGQmlrvqpnIVAKS-----IPFTMEADSLNCCVLGEDItpdqpefalFIREVVREM----TTKAGQ 293
Cdd:cd07087 176 -PFDHIFFTGSPAVGK-------IVMEAaakhlTPVTLELGGKSPCIVDKDA---------NLEVAARRIawgkFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 294 KCTAIRRIIVPQAlvnaVSDALVARLQKVVV---GDPAQEGVKMGALVNAEQradvQEKVNTLLAAGcEIRLGGQADlsA 370
Cdd:cd07087 239 TCIAPDYVLVHES----IKDELIEELKKAIKefyGEDPKESPDYGRIINERH----FDRLASLLDDG-KVVIGGQVD--K 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 371 AGAFFPPTLLYCPQPDEtpAVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIA 440
Cdd:cd07087 308 EERYIAPTILDDVSPDS--PLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLA 375
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
149-416 |
3.33e-12 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 69.40 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDsgLVPEGAISLICGSAGDLLDHLDSQD-- 226
Cdd:cd07116 138 GVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGD--LLPPGVVNVVNGFGLEAGKPLASSKri 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 227 -VVTFTGSAATGQ--MLRVQPNIvaksIPFTMEADSLNCCVLGEDITPDQPEfalFIREVVREMTTKA---GQKCTAIRR 300
Cdd:cd07116 216 aKVAFTGETTTGRliMQYASENI----IPVTLELGGKSPNIFFADVMDADDA---FFDKALEGFVMFAlnqGEVCTCPSR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 301 IIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLS---AAGAFFPP 377
Cdd:cd07116 289 ALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELgglLGGGYYVP 368
|
250 260 270
....*....|....*....|....*....|....*....
gi 1744921533 378 TLLYCPQpdeTPAVHATEAFGPVATLMPAQNQQHALQLA 416
Cdd:cd07116 369 TTFKGGN---KMRIFQEEIFGPVLAVTTFKDEEEALEIA 404
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
64-441 |
4.16e-12 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 68.59 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 64 RAAMLKAVAKhLLSEKER--FYALSAQTGATRADSWVDiegGIGTLFTYASLGSRELpDDTLWPEDELIPLSKeggFAAR 141
Cdd:cd07137 23 RKSQLKGLLR-LVDENEDdiFAALRQDLGKPSAESFRD---EVSVLVSSCKLAIKEL-KKWMAPEKVKTPLTT---FPAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 142 -HVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKP---ATATAQLTQAMVKSIVDSGlvpegAISLICGSAGD 217
Cdd:cd07137 95 aEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPselAPATSALLAKLIPEYLDTK-----AIKVIEGGVPE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 218 ---LLDHldSQDVVTFTGSAATGqmlRVQPNIVAKSI-PFTMEADSlNCCVLGEDITPDQpefALFIREVVREMTTKAGQ 293
Cdd:cd07137 170 ttaLLEQ--KWDKIFFTGSPRVG---RIIMAAAAKHLtPVTLELGG-KCPVIVDSTVDLK---VAVRRIAGGKWGCNNGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 294 KCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGvKMGALVNAEQradvQEKVNTLL---AAGCEIRLGGQADlsA 370
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHH----FQRLSRLLddpSVADKIVHGGERD--E 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1744921533 371 AGAFFPPTLLYCPQPDETpaVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIAD 441
Cdd:cd07137 314 KNLYIEPTILLDPPLDSS--IMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAE 382
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
149-416 |
2.01e-11 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 66.84 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFP----CWgmleKLAPTWLGGMPAIIKPATATAqLTQAMVKSIVDSGLVPEGAISLICG---SAGDLLDH 221
Cdd:PRK09847 159 GVIAAIVPWNFPllltCW----KLGPALAAGNSVILKPSEKSP-LSAIRLAGLAKEAGLPDGVLNVVTGfghEAGQALSR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 222 LDSQDVVTFTGSAATG-QMLRVQPNIVAKSIPFTMEADSLNCcvlgedITPDQPEFALFIREVVREMTTKAGQKCTAIRR 300
Cdd:PRK09847 234 HNDIDAIAFTGSTRTGkQLLKDAGDSNMKRVWLEAGGKSANI------VFADCPDLQQAASATAAGIFYNQGQVCIAGTR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 301 IIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGcEIRLGGQAdlSAAGAFFPPTLL 380
Cdd:PRK09847 308 LLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRN--AGLAAAIGPTIF 384
|
250 260 270
....*....|....*....|....*....|....*.
gi 1744921533 381 YcpQPDETPAVHATEAFGPVATLMPAQNQQHALQLA 416
Cdd:PRK09847 385 V--DVDPNASLSREEIFGPVLVVTRFTSEEQALQLA 418
|
|
| NodN |
cd03450 |
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ... |
532-655 |
7.62e-11 |
|
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear.
Pssm-ID: 239534 [Multi-domain] Cd Length: 149 Bit Score: 60.66 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 532 EELQPGDSLltprrTMTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFvdAGVGPVIA-----N 606
Cdd:cd03450 14 QELGVSDWV-----TVDQERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPALT--PQLFRVEGvkmgvN 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1744921533 607 YGLENLRFIEPVKPGDTiqVRLtckRKTLKkqrSAEEKPTG--VVEWAVEV 655
Cdd:cd03450 87 YGLDKVRFPAPVPVGSR--VRG---RFTLL---SVEELKGGgvQVTLEVTV 129
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
175-449 |
8.61e-11 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 64.48 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 175 GMPAIIK--PA-TATAQLT-QAMVKSIVDSGLvPEGAISLICGSAGD----LLDHLDSQdVVTFTGSAATGQML------ 240
Cdd:cd07129 135 GCPVVVKahPAhPGTSELVaRAIRAALRATGL-PAGVFSLLQGGGREvgvaLVKHPAIK-AVGFTGSRRGGRALfdaaaa 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 241 RVQPnivaksIPFTMEADSLNCCVLGEDITPDQPEfALfIREVVREMTTKAGQKCTAIRRIIVPQalvNAVSDALVARLQ 320
Cdd:cd07129 213 RPEP------IPFYAELGSVNPVFILPGALAERGE-AI-AQGFVGSLTLGAGQFCTNPGLVLVPA---GPAGDAFIAALA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 321 KVVVGDPAQegvkmgALVNAEQRADVQEKVNTLLAA-GCEIRLGGQADLSAAGAffPPTLLYCPQPD--ETPAVHAtEAF 397
Cdd:cd07129 282 EALAAAPAQ------TMLTPGIAEAYRQGVEALAAApGVRVLAGGAAAEGGNQA--APTLFKVDAAAflADPALQE-EVF 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1744921533 398 GPVATLMPAQNQQHALQLACAGGGSLAGTLV--TADPQIARQFIADAARTHGRI 449
Cdd:cd07129 353 GPASLVVRYDDAAELLAVAEALEGQLTATIHgeEDDLALARELLPVLERKAGRL 406
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
39-447 |
2.32e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 63.65 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 39 LDMAAARLFAIEKGAPALRAMTFIERAAMLKA----VAKHLLSEKERFYALSAQTGATRAdswvdIEGGIGTLfTYASLG 114
Cdd:cd07127 90 LAAARAAMPGWRDAGARARAGVCLEILQRLNArsfeMAHAVMHTTGQAFMMAFQAGGPHA-----QDRGLEAV-AYAWRE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 115 SRELPDDTLW--PEDELIPLSKEGGFaarHVLtsKSGVAVHINAFNFPCW----GMLEKLA---PTWLGGMPAIIKPATA 185
Cdd:cd07127 164 MSRIPPTAEWekPQGKHDPLAMEKTF---TVV--PRGVALVIGCSTFPTWngypGLFASLAtgnPVIVKPHPAAILPLAI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 186 TAQLTQAMVKSI-VDSGLVPEGAISLICGSAGDLLDHLDSQdVVTFTGSAATGQMLRVQpniVAKSIPFTmEADSLNCCV 264
Cdd:cd07127 239 TVQVAREVLAEAgFDPNLVTLAADTPEEPIAQTLATRPEVR-IIDFTGSNAFGDWLEAN---ARQAQVYT-EKAGVNTVV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 265 LgeDITPDqpeFALFIREVVREMTTKAGQKCTAIRRIIVP---------QALVNAVSDALVARLQKVVvGDPAQEGVKMG 335
Cdd:cd07127 314 V--DSTDD---LKAMLRNLAFSLSLYSGQMCTTPQNIYVPrdgiqtddgRKSFDEVAADLAAAIDGLL-ADPARAAALLG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 336 ALVNAEQRADVQEKvntllAAGCEIRLGGQAdlsAAGAFFP------PTLLYCPQPDEtpAVHATEAFGPVATLMPAQNQ 409
Cdd:cd07127 388 AIQSPDTLARIAEA-----RQLGEVLLASEA---VAHPEFPdarvrtPLLLKLDASDE--AAYAEERFGPIAFVVATDST 457
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1744921533 410 QHALQLA---CAGGGSLAGTLVTADPQIARQfIADAARTHG 447
Cdd:cd07127 458 DHSIELAresVREHGAMTVGVYSTDPEVVER-VQEAALDAG 497
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1-400 |
1.17e-09 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 61.75 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 1 MQQLASFLSGTWQ-----SGRGRSRLIHHAISGE-ALWEVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKH 74
Cdd:PRK11904 540 AAAIAAFLEKQWQagpiiNGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADL 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 75 LLSEKERFYAL-SAQTGATRADSWVDIEGGIGTLFTYASLGSRELPDDTLW--PEDELIPLSKEGgfaaRhvltsksGVA 151
Cdd:PRK11904 620 LEANRAELIALcVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLpgPTGESNELRLHG----R-------GVF 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 152 VHINAFNFPcwgmlekLApTWLGGMPA--------IIKPATATAQLTQAMVKSIVDSGlVPEGAISLICGSAGDLLDHLD 223
Cdd:PRK11904 689 VCISPWNFP-------LA-IFLGQVAAalaagntvIAKPAEQTPLIAAEAVKLLHEAG-IPKDVLQLLPGDGATVGAALT 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 224 SQ---DVVTFTGSAATGQmlRVQPNIVAKS---IPFTMEADSLNCCVLgeDIT--PDQpefalFIREVVREMTTKAGQKC 295
Cdd:PRK11904 760 ADpriAGVAFTGSTETAR--IINRTLAARDgpiVPLIAETGGQNAMIV--DSTalPEQ-----VVDDVVTSAFRSAGQRC 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 296 TAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGceiRLGGQADLSAA---G 372
Cdd:PRK11904 831 SALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREA---RLLAQLPLPAGtenG 907
|
410 420
....*....|....*....|....*...
gi 1744921533 373 AFFPPTLLYCPQPDETpavhATEAFGPV 400
Cdd:PRK11904 908 HFVAPTAFEIDSISQL----EREVFGPI 931
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
149-416 |
4.60e-09 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 59.16 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKP---ATATAQLTQAMVKSIVDSGL--VPEGAISlicgSAGDLLDHld 223
Cdd:cd07135 110 GVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPselTPHTAALLAELVPKYLDPDAfqVVQGGVP----ETTALLEQ-- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 224 SQDVVTFTGSAATGQmlrvqpnIVAKSipftmEADSLNCCVL---GED---ITPD-QPEFALfiREVVREMTTKAGQKCT 296
Cdd:cd07135 184 KFDKIFYTGSGRVGR-------IIAEA-----AAKHLTPVTLelgGKSpviVTKNaDLELAA--KRILWGKFGNAGQICV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 297 AIRRIIVPQalvnAVSDALVARLQKVV---VGDPAQEGVKMGALVNAEQRADVQEKVNTllaAGCEIRLGGQADlsAAGA 373
Cdd:cd07135 250 APDYVLVDP----SVYDEFVEELKKVLdefYPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGEMD--EATR 320
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1744921533 374 FFPPTLLYCPQPDEtpAVHATEAFGPVATLMPAQNQQHALQLA 416
Cdd:cd07135 321 FIPPTIVSDVSWDD--SLMSEELFGPVLPIIKVDDLDEAIKVI 361
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
149-441 |
1.01e-08 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 58.60 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCwgmlekLAPTWL------GGMPAIIKPATATAQLTQAMVKSIVDSGLvPEGAISLICGSAGDLLDHL 222
Cdd:PLN02419 251 GVCAGICPFNFPA------MIPLWMfpvavtCGNTFILKPSEKDPGASVILAELAMEAGL-PDGVLNIVHGTNDTVNAIC 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 223 DSQDV--VTFTGSAATGQMLRVQPNIVAKSIPFTMEADslNCCVLGEDITPDQPEFALFIREVvremtTKAGQKCTAIRR 300
Cdd:PLN02419 324 DDEDIraVSFVGSNTAGMHIYARAAAKGKRIQSNMGAK--NHGLVLPDANIDATLNALLAAGF-----GAAGQRCMALST 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 301 II-VPQAlvNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADLSAA---GAFFP 376
Cdd:PLN02419 397 VVfVGDA--KSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGyekGNFIG 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1744921533 377 PTLLYCPQPDETpaVHATEAFGPVATLMPAQNQQHALQLACAGGGSLAGTLVTADPQIARQFIAD 441
Cdd:PLN02419 475 PTILSGVTPDME--CYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMD 537
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
44-424 |
1.25e-08 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 57.62 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 44 ARLFAIEK-GAPALRAMTFIERAAMLKAVAKHLLSEKERFY-ALSAQTGATRADswVDIEggigtlftyaslgsrelpdd 121
Cdd:cd07134 1 RRVFAAQQaHALALRASTAAERIAKLKRLKKAILARREEIIaALAADFRKPAAE--VDLT-------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 122 tlwpedELIPLSKEGGFAARH---------------VLTSKS-------GVAVHINAFNFPCWGMLEKLAPTWLGGMPAI 179
Cdd:cd07134 59 ------EILPVLSEINHAIKHlkkwmkpkrvrtpllLFGTKSkiryepkGVCLIISPWNYPFNLAFGPLVSAIAAGNTAI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 180 IKP---ATATAQLTQAMVKSIVDSGLVP--EGAISLicgsAGDLL----DHldsqdvVTFTGSAATGQmlrvqpnIV--- 247
Cdd:cd07134 133 LKPselTPHTSAVIAKIIREAFDEDEVAvfEGDAEV----AQALLelpfDH------IFFTGSPAVGK-------IVmaa 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 248 -AKSI-PFTMEadslnccvLGE------DITPDQPEFAlfiREVVREMTTKAGQKCTAIRRIIVPqalvNAVSDALVARL 319
Cdd:cd07134 196 aAKHLaSVTLE--------LGGksptivDETADLKKAA---KKIAWGKFLNAGQTCIAPDYVFVH----ESVKDAFVEHL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 320 QKVVV-----GDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQADlsAAGAFFPPTLLYCPQPDEtpAVHAT 394
Cdd:cd07134 261 KAEIEkfygkDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD--AAQRYIAPTVLTNVTPDM--KIMQE 336
|
410 420 430
....*....|....*....|....*....|
gi 1744921533 395 EAFGPVATLMPAQNQQHALQLACAGGGSLA 424
Cdd:cd07134 337 EIFGPVLPIITYEDLDEVIEYINAKPKPLA 366
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
173-402 |
3.06e-08 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 56.83 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 173 LGGMPAII------KPATaTAQLTQAMVKSIVDSGLVPEGAISLICGSAGDLLDH-LDSQDV--VTFTGSAATGQML--R 241
Cdd:cd07123 189 LAGAPALMgnvvlwKPSD-TAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTvLASPHLagLHFTGSTPTFKSLwkQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 242 VQPNIVA-KSIPFtmeadslnccVLGEDITPDqpeFALF-----IREVVREMTTKA----GQKCTAIRRIIVPQALVNAV 311
Cdd:cd07123 268 IGENLDRyRTYPR----------IVGETGGKN---FHLVhpsadVDSLVTATVRGAfeyqGQKCSAASRAYVPESLWPEV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 312 SDALVARLQKVVVGDPAQEGVKMGALVnaEQRAdvQEKVNTLL-----AAGCEIRLGGQADLSaAGAFFPPTLLYCPQPD 386
Cdd:cd07123 335 KERLLEELKEIKMGDPDDFSNFMGAVI--DEKA--FDRIKGYIdhaksDPEAEIIAGGKCDDS-VGYFVEPTVIETTDPK 409
|
250
....*....|....*.
gi 1744921533 387 ETPAVhaTEAFGPVAT 402
Cdd:cd07123 410 HKLMT--EEIFGPVLT 423
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
149-414 |
3.25e-08 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 56.58 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKP---ATATAQLTQAMVKSIVDSGLVP--EGAISLIcgsagdllDHLD 223
Cdd:PTZ00381 111 GVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPselSPHTSKLMAKLLTKYLDPSYVRviEGGVEVT--------TELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 224 SQ--DVVTFTGSAATGQmlrvqpnIVAKS-----IPFTMEADSLNCCVLGEDItpdqpEFALFIREVVREMTTKAGQKCT 296
Cdd:PTZ00381 183 KEpfDHIFFTGSPRVGK-------LVMQAaaenlTPCTLELGGKSPVIVDKSC-----NLKVAARRIAWGKFLNAGQTCV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 297 AIRRIIVPQALVNAVSDALvARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTllaAGCEIRLGGQADLSAagAFFP 376
Cdd:PTZ00381 251 APDYVLVHRSIKDKFIEAL-KEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVDIEN--KYVA 324
|
250 260 270
....*....|....*....|....*....|....*...
gi 1744921533 377 PTLLYCPQPDETpaVHATEAFGPVATLMPAQNQQHALQ 414
Cdd:PTZ00381 325 PTIIVNPDLDSP--LMQEEIFGPILPILTYENIDEVLE 360
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
33-400 |
9.59e-08 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 55.64 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 33 EVTSEGLDMAAARLFAIEKGAPALRAMTFIERAAMLKAVAKHLLSEKERFYALSAQ-TGATRADSWVDIEGGIGTLFTYA 111
Cdd:PRK11905 583 TVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVReAGKTLANAIAEVREAVDFLRYYA 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 112 SLGSRELPDDTLWPEdeliplskeggfaarhvltsksGVAVHINAFNFPcwgmlekLApTWLG--------GMPAIIKPA 183
Cdd:PRK11905 663 AQARRLLNGPGHKPL----------------------GPVVCISPWNFP-------LA-IFTGqiaaalvaGNTVLAKPA 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 184 TATAQLTQAMVKSIVDSGlVPEGAISLICGSAGDLLDHL--DSQ-DVVTFTGSAATGQML-RVQPNIVAKSIPFTMEADS 259
Cdd:PRK11905 713 EQTPLIAARAVRLLHEAG-VPKDALQLLPGDGRTVGAALvaDPRiAGVMFTGSTEVARLIqRTLAKRSGPPVPLIAETGG 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 260 LNCCVLgeDIT--PDQpefalFIREVVREMTTKAGQKCTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGAL 337
Cdd:PRK11905 792 QNAMIV--DSSalPEQ-----VVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPV 864
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1744921533 338 VNAEQRADVQEKVNTLLAAGCEIRLGGQADLSAAGAFFPPTLLycpqpdETPAVHA--TEAFGPV 400
Cdd:PRK11905 865 IDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLI------EIDSISDleREVFGPV 923
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
149-400 |
2.27e-07 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 54.59 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 149 GVAVHINAFNFPCWGMLEKLAPTWLGGMPAIIKPATATAQLTQAMVKSIVDSGlVPEGAISLICGSA---GDLLDHLDSQ 225
Cdd:PRK11809 770 GPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAG-VPAGVVQLLPGRGetvGAALVADARV 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 226 DVVTFTGSAATGQMLrvQPNIVA------KSIPFTMEADSLNCCV-----LGEDITPDqpefalfireVVREMTTKAGQK 294
Cdd:PRK11809 849 RGVMFTGSTEVARLL--QRNLAGrldpqgRPIPLIAETGGQNAMIvdssaLTEQVVAD----------VLASAFDSAGQR 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 295 CTAIRRIIVPQALVNAVSDALVARLQKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRlggQADLSAA--- 371
Cdd:PRK11809 917 CSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVF---QAARENSedw 993
|
250 260 270
....*....|....*....|....*....|.
gi 1744921533 372 --GAFFPPTLLYCPQPDETpavhATEAFGPV 400
Cdd:PRK11809 994 qsGTFVPPTLIELDSFDEL----KREVFGPV 1020
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
178-400 |
9.80e-06 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 48.64 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 178 AIIKP---ATATAQLTQAMVKSIVDSGLVpegaiSLICGSAgDL--------LDHLdsqdvvTFTGSAATGQ--MLRVQP 244
Cdd:cd07133 132 VMIKPsefTPRTSALLAELLAEYFDEDEV-----AVVTGGA-DVaaafsslpFDHL------LFTGSTAVGRhvMRAAAE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 245 NIVaksiPFTMEadslnccvLGED----ITPDQPefalfIREVV-REMTTK---AGQKCTAIRRIIVPQALVNAVSDALV 316
Cdd:cd07133 200 NLT----PVTLE--------LGGKspaiIAPDAD-----LAKAAeRIAFGKllnAGQTCVAPDYVLVPEDKLEEFVAAAK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 317 ARLQKV---VVGDPaqegvKMGALVNAEQRADVQEKVNTLLAAGCE-IRLGGQADLSAAGAFFPPTLLYCPQPDEtpAVH 392
Cdd:cd07133 263 AAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARvIELNPAGEDFAATRKLPPTLVLNVTDDM--RVM 335
|
....*...
gi 1744921533 393 ATEAFGPV 400
Cdd:cd07133 336 QEEIFGPI 343
|
|
| SAV4209_like |
cd03453 |
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ... |
548-641 |
1.10e-05 |
|
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.
Pssm-ID: 239537 [Multi-domain] Cd Length: 127 Bit Score: 45.39 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 548 TEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFVLSAAAGLFVD-AGVGPVIANYGlenLRFIEPVKPGDTIQV 626
Cdd:cd03453 13 SRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDwVGDPGRVVSFG---VRFTKPVPVPDTLTC 89
|
90
....*....|....*
gi 1744921533 627 RLTCKRKTLKKQRSA 641
Cdd:cd03453 90 TGIVVEKTVADGEDA 104
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
565-664 |
1.38e-05 |
|
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.
Pssm-ID: 239524 [Multi-domain] Cd Length: 100 Bit Score: 44.39 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 565 AHMDKIAAAESIFGERVVHGYFVLSAAAGLFVDA----GVGPVIANYGLENLRFIEPVKPGDTIQVRLTCKRKTlkkqrs 640
Cdd:cd03440 1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAaarlGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVG------ 74
|
90 100
....*....|....*....|....
gi 1744921533 641 aeekpTGVVEWAVEVFNQHQTPVA 664
Cdd:cd03440 75 -----RSSVTVEVEVRNEDGKLVA 93
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
291-400 |
1.71e-04 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 44.93 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 291 AGQKCTAIRRIIVPQAlvnaVSDALVARL----QKVVVGDPAQEGVKMGALVNAEQRADVQEKVNTLLAAGCEIRLGGQA 366
Cdd:COG4230 822 AGQRCSALRVLCVQED----IADRVLEMLkgamAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLP 897
|
90 100 110
....*....|....*....|....*....|....
gi 1744921533 367 DLSAAGAFFPPTLLYCPQPDETPAvhatEAFGPV 400
Cdd:COG4230 898 EECANGTFVAPTLIEIDSISDLER----EVFGPV 927
|
|
| PRK13693 |
PRK13693 |
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional |
531-618 |
8.00e-03 |
|
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
Pssm-ID: 184249 [Multi-domain] Cd Length: 142 Bit Score: 37.50 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1744921533 531 FEELQPGDSLltPRRT--MTEADIVNFACLSGD----HFYAHMDKIAAAESIfgerVVHGYFVLSAAAGlFVDAGVGP-- 602
Cdd:PRK13693 6 FSSVKVGDQL--PEKTypLTRQDLVNYAGVSGDlnpiHWDDEIAKVVGLDTA----IAHGMLTMGLGGG-YVTSWVGDpg 78
|
90
....*....|....*.
gi 1744921533 603 VIANYgleNLRFIEPV 618
Cdd:PRK13693 79 AVTEY---NVRFTAVV 91
|
|
| |
